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  • Amino Acid Sequence  (80)
  • *Biological Evolution  (58)
  • American Association for the Advancement of Science (AAAS)  (136)
  • American Geophysical Union (AGU)
  • Irkutsk : Ross. Akad. Nauk, Sibirskoe Otd., Inst. Zemnoj Kory
  • Krefeld : Geologischer Dienst Nordhein-Westfalen
  • 2005-2009  (136)
  • 2007  (136)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (136)
  • American Geophysical Union (AGU)
  • Irkutsk : Ross. Akad. Nauk, Sibirskoe Otd., Inst. Zemnoj Kory
  • Krefeld : Geologischer Dienst Nordhein-Westfalen
Years
  • 2005-2009  (136)
Year
  • 1
    Publication Date: 2007-03-17
    Description: Population dynamics and evolutionary change are linked by the fundamental biological processes of birth and death. This means that population growth may correlate with the strength of selection, whereas evolutionary change can leave an ecological signature. We decompose population growth in an age-structured population into contributions from variation in a quantitative trait. We report that the distribution of body sizes within a population of Soay sheep can markedly influence population dynamics, accounting for up to one-fifth of observed population growth. Our results suggest that there is substantial opportunity for evolutionary dynamics to leave an ecological signature and visa versa.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pelletier, Fanie -- Clutton-Brock, Tim -- Pemberton, Josephine -- Tuljapurkar, Shripad -- Coulson, Tim -- P01 AG 22500/AG/NIA NIH HHS/ -- P01 AG022500/AG/NIA NIH HHS/ -- P01 AG022500-04/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2007 Mar 16;315(5818):1571-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology and the Natural Environment Research Council (NERC) Centre for Population Biology, Imperial College London, Silwood Park, Ascot, Berkshire, SL5 7PY, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17363672" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Birth Weight ; Body Size/genetics ; Body Weight/genetics ; Ecology ; Environment ; Female ; *Genetic Variation ; Hindlimb/anatomy & histology ; Male ; Mathematics ; Population Dynamics ; Population Growth ; *Quantitative Trait, Heritable ; Scotland ; *Selection, Genetic ; *Sheep/anatomy & histology/genetics/growth & development ; Weather
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2007-09-29
    Description: The CCR5 co-receptor binds to the HIV-1 gp120 envelope glycoprotein and facilitates HIV-1 entry into cells. Its N terminus is tyrosine-sulfated, as are many antibodies that react with the co-receptor binding site on gp120. We applied nuclear magnetic resonance and crystallographic techniques to analyze the structure of the CCR5 N terminus and that of the tyrosine-sulfated antibody 412d in complex with gp120 and CD4. The conformations of tyrosine-sulfated regions of CCR5 (alpha-helix) and 412d (extended loop) are surprisingly different. Nonetheless, a critical sulfotyrosine on CCR5 and on 412d induces similar structural rearrangements in gp120. These results now provide a framework for understanding HIV-1 interactions with the CCR5 N terminus during viral entry and define a conserved site on gp120, whose recognition of sulfotyrosine engenders posttranslational mimicry by the immune system.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2278242/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2278242/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Chih-Chin -- Lam, Son N -- Acharya, Priyamvada -- Tang, Min -- Xiang, Shi-Hua -- Hussan, Syed Shahzad-Ul -- Stanfield, Robyn L -- Robinson, James -- Sodroski, Joseph -- Wilson, Ian A -- Wyatt, Richard -- Bewley, Carole A -- Kwong, Peter D -- P30 AI060354/AI/NIAID NIH HHS/ -- U19 AI067854/AI/NIAID NIH HHS/ -- U19 AI067854-03/AI/NIAID NIH HHS/ -- Z99 AI999999/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2007 Sep 28;317(5846):1930-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17901336" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, CD4/*chemistry/immunology ; Crystallography, X-Ray ; HIV Antibodies/*chemistry/immunology ; HIV Envelope Protein gp120/*chemistry/immunology/metabolism ; HIV-1/metabolism ; Humans ; Models, Molecular ; Molecular Mimicry ; Molecular Sequence Data ; Nuclear Magnetic Resonance, Biomolecular ; Peptide Fragments/chemistry/metabolism ; Receptors, CCR5/*chemistry/metabolism ; Sulfates/metabolism ; Tyrosine/metabolism ; Virus Internalization
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 2007-12-22
    Description: Beetles represent almost one-fourth of all described species, and knowledge about their relationships and evolution adds to our understanding of biodiversity. We performed a comprehensive phylogenetic analysis of Coleoptera inferred from three genes and nearly 1900 species, representing more than 80% of the world's recognized beetle families. We defined basal relationships in the Polyphaga supergroup, which contains over 300,000 species, and established five families as the earliest branching lineages. By dating the phylogeny, we found that the success of beetles is explained neither by exceptional net diversification rates nor by a predominant role of herbivory and the Cretaceous rise of angiosperms. Instead, the pre-Cretaceous origin of more than 100 present-day lineages suggests that beetle species richness is due to high survival of lineages and sustained diversification in a variety of niches.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hunt, Toby -- Bergsten, Johannes -- Levkanicova, Zuzana -- Papadopoulou, Anna -- John, Oliver St -- Wild, Ruth -- Hammond, Peter M -- Ahrens, Dirk -- Balke, Michael -- Caterino, Michael S -- Gomez-Zurita, Jesus -- Ribera, Ignacio -- Barraclough, Timothy G -- Bocakova, Milada -- Bocak, Ladislav -- Vogler, Alfried P -- New York, N.Y. -- Science. 2007 Dec 21;318(5858):1913-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Entomology, Natural History Museum, Cromwell Road, London SW7 5BD, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18096805" target="_blank"〉PubMed〈/a〉
    Keywords: Angiosperms ; Animals ; Beetles/anatomy & histology/*classification/*genetics/physiology ; Biodiversity ; *Biological Evolution ; Feeding Behavior ; Fossils ; Genes, Insect ; Gymnosperms ; *Phylogeny
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  • 4
    Publication Date: 2007-08-04
    Description: BtuCD is an adenosine triphosphate-binding cassette (ABC) transporter that translocates vitamin B12 from the periplasmic binding protein BtuF into the cytoplasm of Escherichia coli. The 2.6 angstrom crystal structure of a complex BtuCD-F reveals substantial conformational changes as compared with the previously reported structures of BtuCD and BtuF. The lobes of BtuF are spread apart, and B12 is displaced from the binding pocket. The transmembrane BtuC subunits reveal two distinct conformations, and the translocation pathway is closed to both sides of the membrane. Electron paramagnetic resonance spectra of spin-labeled cysteine mutants reconstituted in proteoliposomes are consistent with the conformation of BtuCD-F that was observed in the crystal structure. A comparison with BtuCD and the homologous HI1470/71 protein suggests that the structure of BtuCD-F may reflect a posttranslocation intermediate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hvorup, Rikki N -- Goetz, Birke A -- Niederer, Martina -- Hollenstein, Kaspar -- Perozo, Eduardo -- Locher, Kaspar P -- New York, N.Y. -- Science. 2007 Sep 7;317(5843):1387-90. Epub 2007 Aug 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology and Biophysics, ETH Zurich, HPK D14.3, 8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17673622" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/*chemistry ; Amino Acid Sequence ; Crystallography, X-Ray ; Electron Spin Resonance Spectroscopy ; Escherichia coli ; Escherichia coli Proteins/*chemistry ; Models, Molecular ; Molecular Sequence Data ; Periplasmic Binding Proteins/*chemistry ; Protein Binding ; Protein Conformation ; Recombinant Fusion Proteins/chemistry
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-07-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2007 Jul 6;317(5834):27.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17615309" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Genes ; *Genome ; Genome, Human ; Genomics ; Humans ; Introns ; Sea Anemones/*genetics ; Sequence Analysis, DNA
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-08-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barash, David P -- New York, N.Y. -- Science. 2007 Aug 3;317(5838):596-7; author reply 596-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17673639" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Group Processes ; Humans ; *Morals ; *Psychology, Social
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  • 7
    Publication Date: 2007-10-27
    Description: We report the cloning of Style2.1, the major quantitative trait locus responsible for a key floral attribute (style length) associated with the evolution of self-pollination in cultivated tomatoes. The gene encodes a putative transcription factor that regulates cell elongation in developing styles. The transition from cross-pollination to self-pollination was accompanied, not by a change in the STYLE2.1 protein, but rather by a mutation in the Style2.1 promoter that results in a down-regulation of Style2.1 expression during flower development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Kai-Yi -- Cong, Bin -- Wing, Rod -- Vrebalov, Julia -- Tanksley, Steven D -- New York, N.Y. -- Science. 2007 Oct 26;318(5850):643-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Breeding and Genetics, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17962563" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Biological Evolution ; Chromosome Mapping ; Cloning, Molecular ; Crosses, Genetic ; Down-Regulation ; Flowers/*anatomy & histology/genetics/growth & development ; Genes, Plant ; Genotype ; Helix-Loop-Helix Motifs ; Lycopersicon esculentum/anatomy & histology/*genetics/*physiology ; Molecular Sequence Data ; Plant Proteins/chemistry/*genetics/metabolism ; Pollen/physiology ; Promoter Regions, Genetic ; Quantitative Trait Loci ; Reproduction ; Sequence Deletion ; Transcription Factors/chemistry/*genetics/metabolism ; Transformation, Genetic
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-05-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2007 May 4;316(5825):686-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17478697" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Animals ; Biodiversity ; *Biological Evolution ; *Ecosystem ; Gene Flow ; Geography ; Plants
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-10-27
    Description: Altruism-benefiting fellow group members at a cost to oneself-and parochialism-hostility toward individuals not of one's own ethnic, racial, or other group-are common human behaviors. The intersection of the two-which we term "parochial altruism"-is puzzling from an evolutionary perspective because altruistic or parochial behavior reduces one's payoffs by comparison to what one would gain by eschewing these behaviors. But parochial altruism could have evolved if parochialism promoted intergroup hostilities and the combination of altruism and parochialism contributed to success in these conflicts. Our game-theoretic analysis and agent-based simulations show that under conditions likely to have been experienced by late Pleistocene and early Holocene humans, neither parochialism nor altruism would have been viable singly, but by promoting group conflict, they could have evolved jointly.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Choi, Jung-Kyoo -- Bowles, Samuel -- New York, N.Y. -- Science. 2007 Oct 26;318(5850):636-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Economics and Trade, Kyungpook National University, 1370 Sankyuk-dong, Buk-gu, Daegu 702-701, Korea.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17962562" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; *Altruism ; *Biological Evolution ; Computer Simulation ; Cooperative Behavior ; Female ; Game Theory ; *Hostility ; Humans ; Male ; Models, Psychological ; Reproduction ; *Social Behavior ; *Warfare
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  • 10
    Publication Date: 2007-03-24
    Description: The nucleoporins Nup58 and Nup45 are part of the central transport channel of the nuclear pore complex, which is thought to have a flexible diameter. In the crystal structure of an alpha-helical region of mammalian Nup58/45, we identified distinct tetramers, each consisting of two antiparallel hairpin dimers. The intradimeric interface is hydrophobic, whereas dimer-dimer association occurs through large hydrophilic residues. These residues are laterally displaced in various tetramer conformations, which suggests an intermolecular sliding by 11 angstroms. We propose that circumferential sliding plays a role in adjusting the diameter of the central transport channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Melcak, Ivo -- Hoelz, Andre -- Blobel, Gunter -- R01 GM111461/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Mar 23;315(5819):1729-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17379812" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Membrane Glycoproteins/chemistry ; Molecular Sequence Data ; Nuclear Pore Complex Proteins/*chemistry ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Rats ; Static Electricity
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-03-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2007 Mar 9;315(5817):1352-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17347420" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Biomechanical Phenomena ; Extremities/innervation/physiology ; Mesencephalon/physiology ; Models, Biological ; Models, Neurological ; Muscle Contraction ; Nerve Net/*physiology ; *Robotics ; Salamandra/anatomy & histology/*physiology ; Spinal Cord/*physiology ; Swimming ; *Walking
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-07-28
    Description: Morphological variation within species is a raw material subject to natural selection. However, temporal change in morphological diversity has usually been studied in terms of variation among rather than within species. The distribution of polymorphic traits in cladistic character-taxon matrices reveals that the frequency and extent of morphological variation in 982 trilobite species are greatest early in the evolution of the group: Stratigraphically old and/or phylogenetically basal taxa are significantly more variable than younger and/or more derived taxa. Through its influence on evolutionary tempo, high intraspecific variation may have played a major role in the pronounced Cambrian diversification of trilobites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Webster, Mark -- New York, N.Y. -- Science. 2007 Jul 27;317(5837):499-502.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of the Geophysical Sciences, University of Chicago, 5734 South Ellis Avenue, Chicago, IL 60637, USA. mwebster@geosci.uchicago.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17656721" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arthropods/*anatomy & histology/classification/genetics ; *Biological Evolution ; *Fossils ; Genetic Speciation ; Genetic Variation ; Paleontology ; Phylogeny ; Species Specificity ; Time
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-10-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Behe, Michael J -- New York, N.Y. -- Science. 2007 Oct 12;318(5848):196; author reply 196.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17932270" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antimalarials/pharmacology ; *Biological Evolution ; Drug Resistance/*genetics ; *Mutation ; Plasmodium/drug effects/genetics ; Pyrimethamine/pharmacology ; *Selection, Genetic ; Tetrahydrofolate Dehydrogenase/genetics/metabolism
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  • 14
    Publication Date: 2007-11-17
    Description: In the time between speciation and extinction, a species' ecological and biogeographic footprint-its occupancy-will vary in response to macroecological drivers and historical contingencies. Despite their importance for understanding macroecological processes, general patterns of long-term species occupancy remain largely unknown. We documented the occupancy histories of Cenozoic marine mollusks from New Zealand. For both genera and species, these show a distinct pattern of increase to relatively short-lived peak occupancy at mid-duration, followed by a decline toward extinction. Thus, species at greatest risk for extinction are those that have already been in decline for a substantial period of time. This pattern of protracted rise and fall stands in contrast to that of incumbency, insofar as species show no general tendency to stay near maximal occupancy once established.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Foote, Michael -- Crampton, James S -- Beu, Alan G -- Marshall, Bruce A -- Cooper, Roger A -- Maxwell, Phillip A -- Matcham, Iain -- New York, N.Y. -- Science. 2007 Nov 16;318(5853):1131-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of the Geophysical Sciences, University of Chicago, 5734 South Ellis Avenue, Chicago, IL 60637 USA. mfoote@uchicago.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18006744" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; *Biological Evolution ; *Extinction, Biological ; *Fossils ; *Mollusca ; Population Dynamics ; Seawater ; Time
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  • 15
    Publication Date: 2007-03-24
    Description: Changes in the genes encoding sensory receptor proteins are an essential step in the evolution of new sensory capacities. In primates, trichromatic color vision evolved after changes in X chromosome-linked photopigment genes. To model this process, we studied knock-in mice that expressed a human long-wavelength-sensitive (L) cone photopigment in the form of an X-linked polymorphism. Behavioral tests demonstrated that heterozygous females, whose retinas contained both native mouse pigments and human L pigment, showed enhanced long-wavelength sensitivity and acquired a new capacity for chromatic discrimination. An inherent plasticity in the mammalian visual system thus permits the emergence of a new dimension of sensory experience based solely on gene-driven changes in receptor organization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacobs, Gerald H -- Williams, Gary A -- Cahill, Hugh -- Nathans, Jeremy -- EY002052/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2007 Mar 23;315(5819):1723-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neuroscience Research Institute and Department of Psychology, University of California, Santa Barbara, CA 93106, USA. jacobs@psych.ucsb.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17379811" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Color Perception/*genetics ; Discrimination (Psychology) ; Electroretinography ; Female ; Genetic Engineering ; Heterozygote ; Humans ; Light ; Male ; Mice ; Neuronal Plasticity ; Primates/genetics/physiology ; Retinal Cone Photoreceptor Cells/*physiology ; Retinal Pigments/*genetics/*physiology ; X Chromosome/genetics ; X Chromosome Inactivation
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  • 16
    Publication Date: 2007-10-13
    Description: Chlamydomonas reinhardtii is a unicellular green alga whose lineage diverged from land plants over 1 billion years ago. It is a model system for studying chloroplast-based photosynthesis, as well as the structure, assembly, and function of eukaryotic flagella (cilia), which were inherited from the common ancestor of plants and animals, but lost in land plants. We sequenced the approximately 120-megabase nuclear genome of Chlamydomonas and performed comparative phylogenomic analyses, identifying genes encoding uncharacterized proteins that are likely associated with the function and biogenesis of chloroplasts or eukaryotic flagella. Analyses of the Chlamydomonas genome advance our understanding of the ancestral eukaryotic cell, reveal previously unknown genes associated with photosynthetic and flagellar functions, and establish links between ciliopathy and the composition and function of flagella.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2875087/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2875087/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Merchant, Sabeeha S -- Prochnik, Simon E -- Vallon, Olivier -- Harris, Elizabeth H -- Karpowicz, Steven J -- Witman, George B -- Terry, Astrid -- Salamov, Asaf -- Fritz-Laylin, Lillian K -- Marechal-Drouard, Laurence -- Marshall, Wallace F -- Qu, Liang-Hu -- Nelson, David R -- Sanderfoot, Anton A -- Spalding, Martin H -- Kapitonov, Vladimir V -- Ren, Qinghu -- Ferris, Patrick -- Lindquist, Erika -- Shapiro, Harris -- Lucas, Susan M -- Grimwood, Jane -- Schmutz, Jeremy -- Cardol, Pierre -- Cerutti, Heriberto -- Chanfreau, Guillaume -- Chen, Chun-Long -- Cognat, Valerie -- Croft, Martin T -- Dent, Rachel -- Dutcher, Susan -- Fernandez, Emilio -- Fukuzawa, Hideya -- Gonzalez-Ballester, David -- Gonzalez-Halphen, Diego -- Hallmann, Armin -- Hanikenne, Marc -- Hippler, Michael -- Inwood, William -- Jabbari, Kamel -- Kalanon, Ming -- Kuras, Richard -- Lefebvre, Paul A -- Lemaire, Stephane D -- Lobanov, Alexey V -- Lohr, Martin -- Manuell, Andrea -- Meier, Iris -- Mets, Laurens -- Mittag, Maria -- Mittelmeier, Telsa -- Moroney, James V -- Moseley, Jeffrey -- Napoli, Carolyn -- Nedelcu, Aurora M -- Niyogi, Krishna -- Novoselov, Sergey V -- Paulsen, Ian T -- Pazour, Greg -- Purton, Saul -- Ral, Jean-Philippe -- Riano-Pachon, Diego Mauricio -- Riekhof, Wayne -- Rymarquis, Linda -- Schroda, Michael -- Stern, David -- Umen, James -- Willows, Robert -- Wilson, Nedra -- Zimmer, Sara Lana -- Allmer, Jens -- Balk, Janneke -- Bisova, Katerina -- Chen, Chong-Jian -- Elias, Marek -- Gendler, Karla -- Hauser, Charles -- Lamb, Mary Rose -- Ledford, Heidi -- Long, Joanne C -- Minagawa, Jun -- Page, M Dudley -- Pan, Junmin -- Pootakham, Wirulda -- Roje, Sanja -- Rose, Annkatrin -- Stahlberg, Eric -- Terauchi, Aimee M -- Yang, Pinfen -- Ball, Steven -- Bowler, Chris -- Dieckmann, Carol L -- Gladyshev, Vadim N -- Green, Pamela -- Jorgensen, Richard -- Mayfield, Stephen -- Mueller-Roeber, Bernd -- Rajamani, Sathish -- Sayre, Richard T -- Brokstein, Peter -- Dubchak, Inna -- Goodstein, David -- Hornick, Leila -- Huang, Y Wayne -- Jhaveri, Jinal -- Luo, Yigong -- Martinez, Diego -- Ngau, Wing Chi Abby -- Otillar, Bobby -- Poliakov, Alexander -- Porter, Aaron -- Szajkowski, Lukasz -- Werner, Gregory -- Zhou, Kemin -- Grigoriev, Igor V -- Rokhsar, Daniel S -- Grossman, Arthur R -- GM07185/GM/NIGMS NIH HHS/ -- GM42143/GM/NIGMS NIH HHS/ -- R01 GM032843/GM/NIGMS NIH HHS/ -- R01 GM042143/GM/NIGMS NIH HHS/ -- R01 GM042143-09/GM/NIGMS NIH HHS/ -- R01 GM060992/GM/NIGMS NIH HHS/ -- R01 GM062915-06/GM/NIGMS NIH HHS/ -- R37 GM030626/GM/NIGMS NIH HHS/ -- R37 GM042143/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Oct 12;318(5848):245-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California at Los Angeles, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17932292" target="_blank"〉PubMed〈/a〉
    Keywords: Algal Proteins/*genetics/*physiology ; Animals ; *Biological Evolution ; Chlamydomonas reinhardtii/*genetics/physiology ; Chloroplasts/metabolism ; Computational Biology ; DNA, Algal/genetics ; Flagella/metabolism ; Genes ; *Genome ; Genomics ; Membrane Transport Proteins/genetics/physiology ; Molecular Sequence Data ; Multigene Family ; Photosynthesis/genetics ; Phylogeny ; Plants/genetics ; Proteome ; Sequence Analysis, DNA
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  • 17
    Publication Date: 2007-04-14
    Description: We report crystal structures of the 2.6-megadalton alpha6beta6 heterododecameric fatty acid synthase from Thermomyces lanuginosus at 3.1 angstrom resolution. The alpha and beta polypeptide chains form the six catalytic domains required for fatty acid synthesis and numerous expansion segments responsible for extensive intersubunit connections. Detailed views of all active sites provide insights into substrate specificities and catalytic mechanisms and reveal their unique characteristics, which are due to the integration into the multienzyme. The mode of acyl carrier protein attachment in the reaction chamber, together with the spatial distribution of active sites, suggests that iterative substrate shuttling is achieved by a relatively restricted circular motion of the carrier domain in the multifunctional enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jenni, Simon -- Leibundgut, Marc -- Boehringer, Daniel -- Frick, Christian -- Mikolasek, Bohdan -- Ban, Nenad -- New York, N.Y. -- Science. 2007 Apr 13;316(5822):254-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology and Biophysics, ETH Zurich, 8092 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17431175" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/metabolism ; Acetyltransferases/metabolism ; Acyl Carrier Protein/chemistry/metabolism/ultrastructure ; Acyltransferases/metabolism ; Amino Acid Sequence ; Ascomycota/*enzymology ; Catalytic Domain ; Crystallography, X-Ray ; Enoyl-(Acyl-Carrier-Protein) Reductase (NADH)/metabolism ; Fatty Acid Synthases/*chemistry/metabolism ; Fungal Proteins/*chemistry/metabolism ; Hydro-Lyases/metabolism ; Models, Molecular ; Molecular Sequence Data ; NADP/chemistry ; Protein Conformation ; Protein Subunits/chemistry ; Substrate Specificity
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  • 18
    Publication Date: 2007-03-31
    Description: Plastid-to-nucleus retrograde signaling coordinates nuclear gene expression with chloroplast function and is essential for the photoautotrophic life-style of plants. Three retrograde signals have been described, but little is known of their signaling pathways. We show here that GUN1, a chloroplast-localized pentatricopeptide-repeat protein, and ABI4, an Apetala 2 (AP2)-type transcription factor, are common to all three pathways. ABI4 binds the promoter of a retrograde-regulated gene through a conserved motif found in close proximity to a light-regulatory element. We propose a model in which multiple indicators of aberrant plastid function in Arabidopsis are integrated upstream of GUN1 within plastids, which leads to ABI4-mediated repression of nuclear-encoded genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koussevitzky, Shai -- Nott, Ajit -- Mockler, Todd C -- Hong, Fangxin -- Sachetto-Martins, Gilberto -- Surpin, Marci -- Lim, Jason -- Mittler, Ron -- Chory, Joanne -- DRG-1865-05/PHS HHS/ -- F32 GM 18172/GM/NIGMS NIH HHS/ -- F32 GM 69090/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 May 4;316(5825):715-9. Epub 2007 Mar 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17395793" target="_blank"〉PubMed〈/a〉
    Keywords: Abscisic Acid ; Amino Acid Motifs ; Amino Acid Sequence ; Arabidopsis/genetics/*metabolism ; Arabidopsis Proteins/chemistry/genetics/*metabolism ; Cell Nucleus/*metabolism/*microbiology ; Chloroplasts/*metabolism ; DNA, Plant/metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Electron Transport ; *Gene Expression Regulation, Plant ; Light-Harvesting Protein Complexes/genetics ; Lincomycin/pharmacology ; Models, Biological ; Molecular Sequence Data ; Oligonucleotide Array Sequence Analysis ; Plants, Genetically Modified ; Promoter Regions, Genetic ; Protoporphyrins/metabolism ; Pyridazines/pharmacology ; Signal Transduction ; Transcription Factors/*metabolism
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  • 19
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-09-08
    Description: There is much interest in the evolutionary forces that favored the evolution of large brains in the primate order. The social brain hypothesis posits that selection has favored larger brains and more complex cognitive capacities as a means to cope with the challenges of social life. The hypothesis is supported by evidence that shows that group size is linked to various measures of brain size. But it has not been clear how cognitive complexity confers fitness advantages on individuals. Research in the field and laboratory shows that sophisticated social cognition underlies social behavior in primate groups. Moreover, a growing body of evidence suggests that the quality of social relationships has measurable fitness consequences for individuals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Silk, Joan B -- New York, N.Y. -- Science. 2007 Sep 7;317(5843):1347-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anthropology, University of California, Los Angeles, CA 90095, USA. jsilk@anthro.ucla.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17823344" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Brain/*physiology ; Cognition/physiology ; Humans ; Primates/*physiology ; Reproduction ; Selection, Genetic ; *Social Behavior
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  • 20
    Publication Date: 2007-08-19
    Description: In Gram-negative bacteria and eukaryotic organelles, beta-barrel proteins of the outer membrane protein 85-two-partner secretion B (Omp85-TpsB) superfamily are essential components of protein transport machineries. The TpsB transporter FhaC mediates the secretion of Bordetella pertussis filamentous hemagglutinin (FHA). We report the 3.15 A crystal structure of FhaC. The transporter comprises a 16-stranded beta barrel that is occluded by an N-terminal alpha helix and an extracellular loop and a periplasmic module composed of two aligned polypeptide-transport-associated (POTRA) domains. Functional data reveal that FHA binds to the POTRA 1 domain via its N-terminal domain and likely translocates the adhesin-repeated motifs in an extended hairpin conformation, with folding occurring at the cell surface. General features of the mechanism obtained here are likely to apply throughout the superfamily.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clantin, Bernard -- Delattre, Anne-Sophie -- Rucktooa, Prakash -- Saint, Nathalie -- Meli, Albano C -- Locht, Camille -- Jacob-Dubuisson, Francoise -- Villeret, Vincent -- New York, N.Y. -- Science. 2007 Aug 17;317(5840):957-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉UMR8161 CNRS, Institut de Biologie de Lille, Universite de Lille 1, Universite de Lille 2, 1 rue du Prof. Calmette, F-59021 Lille cedex, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17702945" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/chemistry/*metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Bacterial Outer Membrane Proteins/*chemistry/genetics/*metabolism ; Bordetella pertussis/*chemistry/metabolism ; Cell Membrane/metabolism ; Crystallography, X-Ray ; Hydrophobic and Hydrophilic Interactions ; Lipid Bilayers/chemistry/metabolism ; Membrane Transport Proteins/chemistry/metabolism ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Transport ; Virulence Factors, Bordetella/chemistry/*metabolism
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  • 21
    Publication Date: 2007-12-15
    Description: The assimilation of carbon dioxide (CO2) into organic material is quantitatively the most important biosynthetic process. We discovered that an autotrophic member of the archaeal order Sulfolobales, Metallosphaera sedula, fixed CO2 with acetyl-coenzyme A (acetyl-CoA)/propionyl-CoA carboxylase as the key carboxylating enzyme. In this system, one acetyl-CoA and two bicarbonate molecules were reductively converted via 3-hydroxypropionate to succinyl-CoA. This intermediate was reduced to 4-hydroxybutyrate and converted into two acetyl-CoA molecules via 4-hydroxybutyryl-CoA dehydratase. The key genes of this pathway were found not only in Metallosphaera but also in Sulfolobus, Archaeoglobus, and Cenarchaeum species. Moreover, the Global Ocean Sampling database contains half as many 4-hydroxybutyryl-CoA dehydratase sequences as compared with those found for another key photosynthetic CO2-fixing enzyme, ribulose-1,5-bisphosphate carboxylase-oxygenase. This indicates the importance of this enzyme in global carbon cycling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berg, Ivan A -- Kockelkorn, Daniel -- Buckel, Wolfgang -- Fuchs, Georg -- New York, N.Y. -- Science. 2007 Dec 14;318(5857):1782-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Mikrobiologie, Fakultat Biologie, Universitat Freiburg, Schanzlestrasse 1, D-79104 Freiburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18079405" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyl Coenzyme A/metabolism ; Acetyl-CoA Carboxylase/metabolism ; Acyl Coenzyme A/metabolism ; Amino Acid Sequence ; Anaerobiosis ; Archaea/genetics/metabolism ; Autotrophic Processes ; Bicarbonates/metabolism ; Carbon Dioxide/*metabolism ; Genes, Archaeal ; Hydro-Lyases/genetics/metabolism ; Hydroxybutyrates/*metabolism ; Kinetics ; Lactic Acid/*analogs & derivatives/metabolism ; Metabolic Networks and Pathways ; Molecular Sequence Data ; Oxidation-Reduction ; Photosynthesis ; Phylogeny ; Sulfolobaceae/genetics/*metabolism
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  • 22
    Publication Date: 2007-11-10
    Description: Liu et al. (Reports, 23 March 2007, p. 1712) reported that the Arabidopsis thaliana gene GCR2 encodes a seven-transmembrane, G protein-coupled receptor for abscisic acid. We argue that GCR2 is not likely to be a transmembrane protein nor a G protein-coupled receptor. Instead, GCR2 is most likely a plant homolog of bacterial lanthionine synthetases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnston, Christopher A -- Temple, Brenda R -- Chen, Jin-Gui -- Gao, Yajun -- Moriyama, Etsuko N -- Jones, Alan M -- Siderovski, David P -- Willard, Francis S -- New York, N.Y. -- Science. 2007 Nov 9;318(5852):914; author reply 914.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of North Carolina, Chapel Hill, NC 27599, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17991845" target="_blank"〉PubMed〈/a〉
    Keywords: Abscisic Acid/*metabolism ; Algorithms ; Amino Acid Sequence ; Arabidopsis/chemistry/*metabolism ; Arabidopsis Proteins/*chemistry/isolation & purification/*metabolism ; GTP-Binding Protein alpha Subunits/metabolism ; Hydro-Lyases/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Multienzyme Complexes/*chemistry/metabolism ; Plant Growth Regulators/*metabolism ; Protein Binding ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Receptors, G-Protein-Coupled/*chemistry/isolation & purification/*metabolism ; Recombinant Proteins/chemistry/metabolism ; Sequence Alignment
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  • 23
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-04-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berner, Robert A -- Vandenbrooks, John M -- Ward, Peter D -- New York, N.Y. -- Science. 2007 Apr 27;316(5824):557-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Geology and Geophysics, Yale University, New Haven, CT 06520, USA. robert.berner@yale.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17463279" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Alligators and Crocodiles/embryology ; Animals ; *Atmosphere ; *Biological Evolution ; Body Size ; Drosophila melanogaster/anatomy & histology/physiology ; Embryonic Development ; Extinction, Biological ; Fishes/anatomy & histology/physiology ; Locomotion ; Mollusca/anatomy & histology/physiology ; *Oxygen ; Oxygen Consumption ; Plants/metabolism ; Swimming ; Time ; Vertebrates/anatomy & histology/physiology
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  • 24
    Publication Date: 2007-09-29
    Description: The SAX-3/roundabout (Robo) receptor has SLT-1/Slit-dependent and -independent functions in guiding cell and axon migrations. We identified enhancer of ventral-axon guidance defects of unc-40 mutants (EVA-1) as a Caenorhabditis elegans transmembrane receptor for SLT-1. EVA-1 has two predicted galactose-binding ectodomains, acts cell-autonomously for SLT-1/Slit-dependent axon migration functions of SAX-3/Robo, binds to SLT-1 and SAX-3, colocalizes with SAX-3 on cells, and provides cell specificity to the activation of SAX-3 signaling by SLT-1. Double mutants of eva-1 or slt-1 with sax-3 mutations suggest that SAX-3 can (when slt-1 or eva-1 function is reduced) inhibit a parallel-acting guidance mechanism, which involves UNC-40/deleted in colorectal cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fujisawa, Kazuko -- Wrana, Jeffrey L -- Culotti, Joseph G -- NS41397/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2007 Sep 28;317(5846):1934-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Samuel Lunenfeld Research Institute of Mount Sinai Hospital, 600 University Avenue, Toronto, Ontario M5G 1X5, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17901337" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Axons/*physiology ; Caenorhabditis elegans/cytology/genetics/growth & development/*physiology ; Caenorhabditis elegans Proteins/*chemistry/genetics/*metabolism ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Line ; Cell Movement ; Cloning, Molecular ; Humans ; Molecular Sequence Data ; Mutation ; Nerve Tissue Proteins/*metabolism ; Nervous System/growth & development/metabolism ; Neurons/physiology ; Protein Structure, Tertiary ; Receptors, Immunologic/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction
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  • 25
    Publication Date: 2007-05-26
    Description: Mutations affecting the BRCT domains of the breast cancer-associated tumor suppressor BRCA1 disrupt the recruitment of this protein to DNA double-strand breaks (DSBs). The molecular structures at DSBs recognized by BRCA1 are presently unknown. We report the interaction of the BRCA1 BRCT domain with RAP80, a ubiquitin-binding protein. RAP80 targets a complex containing the BRCA1-BARD1 (BRCA1-associated ring domain protein 1) E3 ligase and the deubiquitinating enzyme (DUB) BRCC36 to MDC1-gammaH2AX-dependent lysine(6)- and lysine(63)-linked ubiquitin polymers at DSBs. These events are required for cell cycle checkpoint and repair responses to ionizing radiation, implicating ubiquitin chain recognition and turnover in the BRCA1-mediated repair of DSBs.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2706583/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2706583/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sobhian, Bijan -- Shao, Genze -- Lilli, Dana R -- Culhane, Aedin C -- Moreau, Lisa A -- Xia, Bing -- Livingston, David M -- Greenberg, Roger A -- K08 CA106597/CA/NCI NIH HHS/ -- K08 CA106597-01A2/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2007 May 25;316(5828):1198-202.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute and Department of Genetics and Department of Medicine, Harvard Medical School, 44 Binney Street, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17525341" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; BRCA1 Protein/*metabolism ; Binding Sites ; Carrier Proteins/*metabolism ; Cell Line ; DNA/*metabolism ; *DNA Breaks, Double-Stranded ; DNA Repair/physiology ; HeLa Cells ; Humans ; Mice ; Molecular Sequence Data ; Nuclear Proteins/*metabolism ; Nucleic Acid Conformation ; Protein Structure, Tertiary ; Tumor Suppressor Proteins/metabolism ; Ubiquitin/*metabolism ; Ubiquitin-Protein Ligases/metabolism
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  • 26
    Publication Date: 2007-11-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jorgensen, Christian -- Enberg, Katja -- Dunlop, Erin S -- Arlinghaus, Robert -- Boukal, David S -- Brander, Keith -- Ernande, Bruno -- Gardmark, Anna -- Johnston, Fiona -- Matsumura, Shuichi -- Pardoe, Heidi -- Raab, Kristina -- Silva, Alexandra -- Vainikka, Anssi -- Dieckmann, Ulf -- Heino, Mikko -- Rijnsdorp, Adriaan D -- New York, N.Y. -- Science. 2007 Nov 23;318(5854):1247-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Bergen, N-5020 Bergen. christian.jorgensen@bio.uib.no〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18033868" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Ecosystem ; *Fisheries/methods ; *Fishes/physiology ; Population Dynamics
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  • 27
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-06-02
    Description: The first appearances of aragonite and calcite skeletons in 18 animal clades that independently evolved mineralization during the late Ediacaran through the Ordovician (approximately 550 to 444 million years ago) correspond to intervals when seawater chemistry favored aragonite and calcite precipitation, respectively. Skeletal mineralogies rarely changed once skeletons evolved, despite subsequent changes in seawater chemistry. Thus, the selection of carbonate skeletal minerals appears to have been dictated by seawater chemistry at the time a clade first acquired its mineralized skeleton.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Porter, Susannah M -- New York, N.Y. -- Science. 2007 Jun 1;316(5829):1302.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth Science, University of California at Santa Barbara, Santa Barbara, CA 93106, USA. porter@geol.ucsb.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17540895" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Calcification, Physiologic ; Calcium/analysis ; Calcium Carbonate/*analysis ; Chemical Precipitation ; Crystallization ; *Fossils ; Invertebrates/*chemistry ; Magnesium/analysis ; Seawater/*chemistry
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  • 28
    Publication Date: 2007-10-13
    Description: Theory suggests it should be difficult for asexual organisms to adapt to a changing environment because genetic diversity can only arise from mutations accumulating within direct antecedents and not through sexual exchange. In an asexual microinvertebrate, the bdelloid rotifer, we have observed a mechanism by which such organisms could acquire the diversity needed for adaptation. Gene copies most likely representing former alleles have diverged in function so that the proteins they encode play complementary roles in survival of dry conditions. One protein prevents desiccation-sensitive enzymes from aggregating during drying, whereas its counterpart does not have this activity, but is able to associate with phospholipid bilayers and is potentially involved in maintenance of membrane integrity. The functional divergence of former alleles observed here suggests that adoption of asexual reproduction could itself be an evolutionary mechanism for the generation of diversity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pouchkina-Stantcheva, Natalia N -- McGee, Brian M -- Boschetti, Chiara -- Tolleter, Dimitri -- Chakrabortee, Sohini -- Popova, Antoaneta V -- Meersman, Filip -- Macherel, David -- Hincha, Dirk K -- Tunnacliffe, Alan -- New York, N.Y. -- Science. 2007 Oct 12;318(5848):268-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Biotechnology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17932297" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; *Alleles ; Amino Acid Sequence ; Animals ; Biological Evolution ; Chromosomes/genetics ; DNA, Complementary ; Dehydration ; Gene Dosage ; *Genes, Helminth ; *Genetic Variation ; Helminth Proteins/chemistry/genetics/*physiology ; Lipid Bilayers ; Molecular Sequence Data ; Protein Structure, Secondary ; *Reproduction, Asexual ; Rotifera/*genetics/*physiology
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  • 29
    Publication Date: 2007-06-30
    Description: As a step toward propagation of synthetic genomes, we completely replaced the genome of a bacterial cell with one from another species by transplanting a whole genome as naked DNA. Intact genomic DNA from Mycoplasma mycoides large colony (LC), virtually free of protein, was transplanted into Mycoplasma capricolum cells by polyethylene glycol-mediated transformation. Cells selected for tetracycline resistance, carried by the M. mycoides LC chromosome, contain the complete donor genome and are free of detectable recipient genomic sequences. These cells that result from genome transplantation are phenotypically identical to the M. mycoides LC donor strain as judged by several criteria.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lartigue, Carole -- Glass, John I -- Alperovich, Nina -- Pieper, Rembert -- Parmar, Prashanth P -- Hutchison, Clyde A 3rd -- Smith, Hamilton O -- Venter, J Craig -- New York, N.Y. -- Science. 2007 Aug 3;317(5838):632-8. Epub 2007 Jun 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉J. Craig Venter Institute, Rockville, MD 20850, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17600181" target="_blank"〉PubMed〈/a〉
    Keywords: Acetate Kinase/chemistry/genetics ; Amino Acid Sequence ; DNA, Bacterial/*genetics/isolation & purification ; *Genome, Bacterial ; Genotype ; Molecular Sequence Data ; Mycoplasma/chemistry/*genetics ; Mycoplasma mycoides/chemistry/*genetics ; Phenotype ; Polyethylene Glycols ; Proteome/analysis ; Recombination, Genetic ; Sequence Analysis, DNA ; *Transformation, Bacterial
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  • 30
    Publication Date: 2007-05-26
    Description: To understand the constraints on biological diversity, we analyzed how selection and development interact to control the evolution of inflorescences, the branching structures that bear flowers. We show that a single developmental model accounts for the restricted range of inflorescence types observed in nature and that this model is supported by molecular genetic studies. The model predicts associations between inflorescence architecture, climate, and life history, which we validated empirically. Paths, or evolutionary wormholes, link different architectures in a multidimensional fitness space, but the rate of evolution along these paths is constrained by genetic and environmental factors, which explains why some evolutionary transitions are rare between closely related plant taxa.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prusinkiewicz, Przemyslaw -- Erasmus, Yvette -- Lane, Brendan -- Harder, Lawrence D -- Coen, Enrico -- New York, N.Y. -- Science. 2007 Jun 8;316(5830):1452-6. Epub 2007 May 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Computer Science, University of Calgary, 2500 University Drive N.W. Calgary, Alberta T2N 1N4, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17525303" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*anatomy & histology/genetics/*growth & development ; Arabidopsis Proteins/genetics/physiology ; *Biological Evolution ; Climate ; Computer Simulation ; Flowers/*anatomy & histology/genetics/*growth & development ; Gene Expression ; Genes, Plant ; Mathematics ; Meristem/growth & development ; *Models, Biological ; Selection, Genetic ; Transcription Factors/genetics/physiology
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  • 31
    Publication Date: 2007-07-14
    Description: Many human cancers involve up-regulation of the phosphoinositide 3-kinase PI3Kalpha, with oncogenic mutations identified in both the p110alpha catalytic and the p85alpha regulatory subunits. We used crystallographic and biochemical approaches to gain insight into activating mutations in two noncatalytic p110alpha domains-the adaptor-binding and the helical domains. A structure of the adaptor-binding domain of p110alpha in a complex with the p85alpha inter-Src homology 2 (inter-SH2) domain shows that oncogenic mutations in the adaptor-binding domain are not at the inter-SH2 interface but in a polar surface patch that is a plausible docking site for other domains in the holo p110/p85 complex. We also examined helical domain mutations and found that the Glu545 to Lys545 (E545K) oncogenic mutant disrupts an inhibitory charge-charge interaction with the p85 N-terminal SH2 domain. These studies extend our understanding of the architecture of PI3Ks and provide insight into how two classes of mutations that cause a gain in function can lead to cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miled, Nabil -- Yan, Ying -- Hon, Wai-Ching -- Perisic, Olga -- Zvelebil, Marketa -- Inbar, Yuval -- Schneidman-Duhovny, Dina -- Wolfson, Haim J -- Backer, Jonathan M -- Williams, Roger L -- GM55692/GM/NIGMS NIH HHS/ -- MC_U105184308/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2007 Jul 13;317(5835):239-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17626883" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; *Catalytic Domain ; Cattle ; Cell Line ; Cell Transformation, Neoplastic ; Crystallography, X-Ray ; Dimerization ; Humans ; Models, Molecular ; Molecular Sequence Data ; *Mutation ; Neoplasms/*genetics ; Phosphatidylinositol 3-Kinases/antagonists & ; inhibitors/chemistry/*genetics/*metabolism ; Protein Structure, Secondary ; Protein Structure, Tertiary ; src Homology Domains
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  • 32
    Publication Date: 2007-09-29
    Description: The importance of trophic ecology in adaptation and evolution is well known, yet direct evidence that feeding controls microevolution over extended evolutionary time scales, available only from the fossil record, is conspicuously lacking. Through quantitative analysis of tooth microwear, we show that rapid evolutionary change in Miocene stickleback was associated with shifts in feeding, providing direct evidence from the fossil record for changes in trophic niche and resource exploitation driving directional, microevolutionary change over thousands of years. These results demonstrate the potential for tooth microwear analysis to provide powerful insights into trophic ecology during aquatic adaptive radiations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Purnell, Mark A -- Bell, Michael A -- Baines, David C -- Hart, Paul J B -- Travis, Matthew P -- New York, N.Y. -- Science. 2007 Sep 28;317(5846):1887.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Geology, University of Leicester, Leicester LE1 7RH, UK. mark.purnell@leicester.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17901325" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Animals ; *Biological Evolution ; *Diet ; Ecosystem ; *Fossils ; Paleodontology ; Phenotype ; *Smegmamorpha/anatomy & histology ; Tooth/*ultrastructure ; Tooth Attrition
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  • 33
    Publication Date: 2007-03-31
    Description: Telomerase is a ribonucleoprotein enzyme complex that adds 5'-TTAGGG-3' repeats onto the ends of human chromosomes, providing a telomere maintenance mechanism for approximately 90% of human cancers. We have purified human telomerase approximately 10(8)-fold, with the final elution dependent on the enzyme's ability to catalyze nucleotide addition onto a DNA oligonucleotide of telomeric sequence, thereby providing specificity for catalytically active telomerase. Mass spectrometric sequencing of the protein components and molecular size determination indicated an enzyme composition of two molecules each of telomerase reverse transcriptase, telomerase RNA, and dyskerin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, Scott B -- Graham, Mark E -- Lovrecz, George O -- Bache, Nicolai -- Robinson, Phillip J -- Reddel, Roger R -- New York, N.Y. -- Science. 2007 Mar 30;315(5820):1850-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research Unit, Children's Medical Research Institute, 214 Hawkesbury Road, Westmead NSW 2145, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17395830" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Cycle Proteins/*chemistry/isolation & purification ; Cell Line ; Cell Line, Tumor ; Centrifugation, Density Gradient ; Humans ; Molecular Sequence Data ; Molecular Weight ; Multienzyme Complexes/chemistry ; Nuclear Proteins/*chemistry/isolation & purification ; RNA/*chemistry/isolation & purification ; Tandem Mass Spectrometry ; Telomerase/*chemistry/isolation & purification/metabolism
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  • 34
    Publication Date: 2007-07-07
    Description: Sea anemones are seemingly primitive animals that, along with corals, jellyfish, and hydras, constitute the oldest eumetazoan phylum, the Cnidaria. Here, we report a comparative analysis of the draft genome of an emerging cnidarian model, the starlet sea anemone Nematostella vectensis. The sea anemone genome is complex, with a gene repertoire, exon-intron structure, and large-scale gene linkage more similar to vertebrates than to flies or nematodes, implying that the genome of the eumetazoan ancestor was similarly complex. Nearly one-fifth of the inferred genes of the ancestor are eumetazoan novelties, which are enriched for animal functions like cell signaling, adhesion, and synaptic transmission. Analysis of diverse pathways suggests that these gene "inventions" along the lineage leading to animals were likely already well integrated with preexisting eukaryotic genes in the eumetazoan progenitor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Putnam, Nicholas H -- Srivastava, Mansi -- Hellsten, Uffe -- Dirks, Bill -- Chapman, Jarrod -- Salamov, Asaf -- Terry, Astrid -- Shapiro, Harris -- Lindquist, Erika -- Kapitonov, Vladimir V -- Jurka, Jerzy -- Genikhovich, Grigory -- Grigoriev, Igor V -- Lucas, Susan M -- Steele, Robert E -- Finnerty, John R -- Technau, Ulrich -- Martindale, Mark Q -- Rokhsar, Daniel S -- 5 P41 LM006252-09/LM/NLM NIH HHS/ -- THL007279F/PHS HHS/ -- New York, N.Y. -- Science. 2007 Jul 6;317(5834):86-94.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Energy Joint Genome Institute, Walnut Creek, CA 94598, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17615350" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Cell Adhesion ; Evolution, Molecular ; Genes ; Genetic Linkage ; *Genome ; Genome, Human ; Genomics ; Humans ; Introns ; Metabolic Networks and Pathways ; Multigene Family ; Muscles/physiology ; Nervous System Physiological Phenomena ; Phylogeny ; Sea Anemones/*genetics/metabolism ; Sequence Analysis, DNA ; Signal Transduction ; Synteny
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  • 35
    Publication Date: 2007-07-21
    Description: PDZ domains have long been thought to cluster into discrete functional classes defined by their peptide-binding preferences. We used protein microarrays and quantitative fluorescence polarization to characterize the binding selectivity of 157 mouse PDZ domains with respect to 217 genome-encoded peptides. We then trained a multidomain selectivity model to predict PDZ domain-peptide interactions across the mouse proteome with an accuracy that exceeds many large-scale, experimental investigations of protein-protein interactions. Contrary to the current paradigm, PDZ domains do not fall into discrete classes; instead, they are evenly distributed throughout selectivity space, which suggests that they have been optimized across the proteome to minimize cross-reactivity. We predict that focusing on families of interaction domains, which facilitates the integration of experimentation and modeling, will play an increasingly important role in future investigations of protein function.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2674608/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2674608/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stiffler, Michael A -- Chen, Jiunn R -- Grantcharova, Viara P -- Lei, Ying -- Fuchs, Daniel -- Allen, John E -- Zaslavskaia, Lioudmila A -- MacBeath, Gavin -- 1 RO1 GM072872-01/GM/NIGMS NIH HHS/ -- 5 T32 GM07598-25/GM/NIGMS NIH HHS/ -- R01 GM072872/GM/NIGMS NIH HHS/ -- R01 GM072872-04/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Jul 20;317(5836):364-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17641200" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Amino Acid Sequence ; Animals ; Computational Biology ; Computer Simulation ; Fluorescence Polarization ; Mice ; Peptides/*metabolism ; Protein Array Analysis ; Protein Binding ; *Protein Structure, Tertiary ; Proteome/chemistry/*metabolism
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  • 36
    Publication Date: 2007-08-11
    Description: Tricyclic antidepressants exert their pharmacological effect-inhibiting the reuptake of serotonin, norepinephrine, and dopamine-by directly blocking neurotransmitter transporters (SERT, NET, and DAT, respectively) in the presynaptic membrane. The drug-binding site and the mechanism of this inhibition are poorly understood. We determined the crystal structure at 2.9 angstroms of the bacterial leucine transporter (LeuT), a homolog of SERT, NET, and DAT, in complex with leucine and the antidepressant desipramine. Desipramine binds at the inner end of the extracellular cavity of the transporter and is held in place by a hairpin loop and by a salt bridge. This binding site is separated from the leucine-binding site by the extracellular gate of the transporter. By directly locking the gate, desipramine prevents conformational changes and blocks substrate transport. Mutagenesis experiments on human SERT and DAT indicate that both the desipramine-binding site and its inhibition mechanism are probably conserved in the human neurotransmitter transporters.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3711652/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3711652/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, Zheng -- Zhen, Juan -- Karpowich, Nathan K -- Goetz, Regina M -- Law, Christopher J -- Reith, Maarten E A -- Wang, Da-Neng -- DA013261/DA/NIDA NIH HHS/ -- DA019676/DA/NIDA NIH HHS/ -- GM075026/GM/NIGMS NIH HHS/ -- GM075936/GM/NIGMS NIH HHS/ -- R01 DA013261/DA/NIDA NIH HHS/ -- R01 DA019676/DA/NIDA NIH HHS/ -- R01 DK053973/DK/NIDDK NIH HHS/ -- R21 DK060841/DK/NIDDK NIH HHS/ -- R21 GM075936/GM/NIGMS NIH HHS/ -- U54 GM075026/GM/NIGMS NIH HHS/ -- U54 GM095315/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Sep 7;317(5843):1390-3. Epub 2007 Aug 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Kimmel Center for Biology and Medicine at the Skirball Institute of Biomolecular Medicine and Department of Cell Biology, New York University School of Medicine, 540 First Avenue, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17690258" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antidepressive Agents, Tricyclic/chemistry/*metabolism ; Bacterial Proteins/chemistry/*metabolism ; Binding Sites ; Caenorhabditis elegans Proteins/chemistry/metabolism ; Cell Line ; Conserved Sequence ; Crystallography, X-Ray ; Desipramine/chemistry/*metabolism ; Dopamine/chemistry/metabolism ; Dopamine Uptake Inhibitors/chemistry/metabolism ; Drosophila Proteins/chemistry/metabolism ; Humans ; Leucine/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Neurotransmitter Uptake Inhibitors/chemistry/*metabolism ; Norepinephrine/chemistry/metabolism ; Norepinephrine Plasma Membrane Transport Proteins/antagonists & ; inhibitors/chemistry/metabolism ; Plasma Membrane Neurotransmitter Transport Proteins/chemistry/*metabolism ; Protein Binding ; Protein Conformation ; Sequence Homology, Amino Acid ; Serotonin/chemistry/metabolism ; Serotonin Uptake Inhibitors/chemistry/metabolism
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  • 37
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-09-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, Ann -- New York, N.Y. -- Science. 2007 Sep 21;317(5845):1664.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17885102" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Animals ; *Biological Evolution ; Body Size ; Bone and Bones ; Female ; *Fossils ; Georgia (Republic) ; *Hominidae/classification ; Humans ; Male
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  • 38
    Publication Date: 2007-12-08
    Description: Many bacterial pathogens have long, slender pili through which they adhere to host cells. The crystal structure of the major pilin subunit from the Gram-positive human pathogen Streptococcus pyogenes at 2.2 angstroms resolution reveals an extended structure comprising two all-beta domains. The molecules associate in columns through the crystal, with each carboxyl terminus adjacent to a conserved lysine of the next molecule. This lysine forms the isopeptide bonds that link the subunits in native pili, validating the relevance of the crystal assembly. Each subunit contains two lysine-asparagine isopeptide bonds generated by an intramolecular reaction, and we find evidence for similar isopeptide bonds in other cell surface proteins of Gram-positive bacteria. The present structure explains the strength and stability of such Gram-positive pili and could facilitate vaccine development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kang, Hae Joo -- Coulibaly, Fasseli -- Clow, Fiona -- Proft, Thomas -- Baker, Edward N -- New York, N.Y. -- Science. 2007 Dec 7;318(5856):1625-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Maurice Wilkins Centre for Molecular Biodiscovery, University of Auckland, Auckland 1010, New Zealand.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18063798" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Asparagine/chemistry ; Chemistry, Physical ; Crystallography, X-Ray ; Fimbriae Proteins/*chemistry ; Fimbriae, Bacterial/*chemistry/ultrastructure ; Hydrogen Bonding ; Lysine/chemistry ; Models, Molecular ; Molecular Sequence Data ; Peptides/chemistry ; Physicochemical Phenomena ; Protein Conformation ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Streptococcus pyogenes/*chemistry/metabolism/*ultrastructure
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  • 39
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-03-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zimmer, Carl -- New York, N.Y. -- Science. 2007 Mar 9;315(5817):1358-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17347424" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Birds/*genetics/metabolism ; *Cell Size ; DNA, Intergenic ; Dinosaurs/*genetics/metabolism ; *Fossils ; *Genome ; Genome, Human ; Humans ; Interspersed Repetitive Sequences ; Osteocytes/cytology ; Selection, Genetic ; Species Specificity
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  • 40
    Publication Date: 2007-01-27
    Description: Vitamin A has diverse biological functions. It is transported in the blood as a complex with retinol binding protein (RBP), but the molecular mechanism by which vitamin A is absorbed by cells from the vitamin A-RBP complex is not clearly understood. We identified in bovine retinal pigment epithelium cells STRA6, a multitransmembrane domain protein, as a specific membrane receptor for RBP. STRA6 binds to RBP with high affinity and has robust vitamin A uptake activity from the vitamin A-RBP complex. It is widely expressed in embryonic development and in adult organ systems. The RBP receptor represents a major physiological mediator of cellular vitamin A uptake.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawaguchi, Riki -- Yu, Jiamei -- Honda, Jane -- Hu, Jane -- Whitelegge, Julian -- Ping, Peipei -- Wiita, Patrick -- Bok, Dean -- Sun, Hui -- 5T32EY07026/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2007 Feb 9;315(5813):820-5. Epub 2007 Jan 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, David Geffen School of Medicine at UCLA, 650 Charles E. Young Drive South, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17255476" target="_blank"〉PubMed〈/a〉
    Keywords: Acyltransferases/metabolism ; Amino Acid Sequence ; Animals ; Blood-Retinal Barrier ; COS Cells ; Cattle ; Cell Line ; Cell Line, Tumor ; Cell Membrane/metabolism ; Cercopithecus aethiops ; Embryonic Development ; Endocytosis ; Humans ; Molecular Sequence Data ; Mutation, Missense ; Pigment Epithelium of Eye/*metabolism ; Placenta/metabolism ; Receptors, Cell Surface/*metabolism ; Retinal Vessels/metabolism ; Retinol-Binding Proteins/*metabolism ; Spleen/metabolism ; Transfection ; Vitamin A/*metabolism
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  • 41
    Publication Date: 2007-10-27
    Description: Pathogenicity of many Gram-negative bacteria relies on the injection of effector proteins by type III secretion into eukaryotic cells, where they modulate host signaling pathways to the pathogen's benefit. One such effector protein injected by Xanthomonas into plants is AvrBs3, which localizes to the plant cell nucleus and causes hypertrophy of plant mesophyll cells. We show that AvrBs3 induces the expression of a master regulator of cell size, upa20, which encodes a transcription factor containing a basic helix-loop-helix domain. AvrBs3 binds to a conserved element in the upa20 promoter via its central repeat region and induces gene expression through its activation domain. Thus, AvrBs3 and likely other members of this family provoke developmental reprogramming of host cells by mimicking eukaryotic transcription factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kay, Sabine -- Hahn, Simone -- Marois, Eric -- Hause, Gerd -- Bonas, Ulla -- New York, N.Y. -- Science. 2007 Oct 26;318(5850):648-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Biology, Department of Genetics, Martin-Luther-University Halle-Wittenberg, Weinbergweg 10, D-06120 Halle (Saale), Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17962565" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/chemistry/genetics/*physiology ; Basic Helix-Loop-Helix Transcription Factors/chemistry/genetics/*physiology ; Capsicum/cytology/*genetics/*microbiology ; Cell Enlargement ; Cell Size ; Chromatin Immunoprecipitation ; Gene Expression Regulation, Plant ; Gene Silencing ; Molecular Sequence Data ; Plant Leaves/cytology/genetics/metabolism ; Plant Proteins/chemistry/genetics/metabolism/*physiology ; Promoter Regions, Genetic ; Tobacco/genetics ; Transcription, Genetic ; Xanthomonas campestris/genetics/*metabolism/pathogenicity
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  • 42
    Publication Date: 2007-04-14
    Description: In the multifunctional fungal fatty acid synthase (FAS), the acyl carrier protein (ACP) domain shuttles reaction intermediates covalently attached to its prosthetic phosphopantetheine group between the different enzymatic centers of the reaction cycle. Here, we report the structure of the Saccharomyces cerevisiae FAS determined at 3.1 angstrom resolution with its ACP stalled at the active site of ketoacyl synthase. The ACP contacts the base of the reaction chamber through conserved, charge-complementary surfaces, which optimally position the ACP toward the catalytic cleft of ketoacyl synthase. The conformation of the prosthetic group suggests a switchblade mechanism for acyl chain delivery to the active site of the enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leibundgut, Marc -- Jenni, Simon -- Frick, Christian -- Ban, Nenad -- New York, N.Y. -- Science. 2007 Apr 13;316(5822):288-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology and Biophysics, ETH Zurich, 8092 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17431182" target="_blank"〉PubMed〈/a〉
    Keywords: Acyl Carrier Protein/*chemistry/metabolism ; Acyltransferases/metabolism ; Amino Acid Sequence ; Catalytic Domain ; Crystallography, X-Ray ; Fatty Acid Synthases/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Saccharomyces cerevisiae Proteins/*chemistry/metabolism
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  • 43
    Publication Date: 2007-05-19
    Description: The Neurospora crassa photoreceptor Vivid tunes blue-light responses and modulates gating of the circadian clock. Crystal structures of dark-state and light-state Vivid reveal a light, oxygen, or voltage Per-Arnt-Sim domain with an unusual N-terminal cap region and a loop insertion that accommodates the flavin cofactor. Photoinduced formation of a cystein-flavin adduct drives flavin protonation to induce an N-terminal conformational change. A cysteine-to-serine substitution remote from the flavin adenine dinucleotide binding site decouples conformational switching from the flavin photocycle and prevents Vivid from sending signals in Neurospora. Key elements of this activation mechanism are conserved by other photosensors such as White Collar-1, ZEITLUPE, ENVOY, and flavin-binding, kelch repeat, F-BOX 1 (FKF1).〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3682417/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3682417/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zoltowski, Brian D -- Schwerdtfeger, Carsten -- Widom, Joanne -- Loros, Jennifer J -- Bilwes, Alexandrine M -- Dunlap, Jay C -- Crane, Brian R -- GM079879-01/GM/NIGMS NIH HHS/ -- MH44651/MH/NIMH NIH HHS/ -- P01 GM068087/GM/NIGMS NIH HHS/ -- R01 GM034985/GM/NIGMS NIH HHS/ -- R01 GM034985-24/GM/NIGMS NIH HHS/ -- R37GM34985/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 May 18;316(5827):1054-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17510367" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Amino Acid Sequence ; Amino Acid Substitution ; Binding Sites ; Crystallography, X-Ray ; Darkness ; Dimerization ; Flavin-Adenine Dinucleotide/chemistry ; Fungal Proteins/*chemistry/genetics/metabolism ; Light ; Molecular Sequence Data ; Mutagenesis ; Neurospora crassa/*chemistry ; Protein Conformation ; Protein Structure, Tertiary
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  • 44
    Publication Date: 2007-11-10
    Description: Production of type I interferon (IFN-I) is a critical host defense triggered by pattern-recognition receptors (PRRs) of the innate immune system. Deubiquitinating enzyme A (DUBA), an ovarian tumor domain-containing deubiquitinating enzyme, was discovered in a small interfering RNA-based screen as a regulator of IFN-I production. Reduction of DUBA augmented the PRR-induced IFN-I response, whereas ectopic expression of DUBA had the converse effect. DUBA bound tumor necrosis factor receptor-associated factor 3 (TRAF3), an adaptor protein essential for the IFN-I response. TRAF3 is an E3 ubiquitin ligase that preferentially assembled lysine-63-linked polyubiquitin chains. DUBA selectively cleaved the lysine-63-linked polyubiquitin chains on TRAF3, resulting in its dissociation from the downstream signaling complex containing TANK-binding kinase 1. A discrete ubiquitin interaction motif within DUBA was required for efficient deubiquitination of TRAF3 and optimal suppression of IFN-I. Our data identify DUBA as a negative regulator of innate immune responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kayagaki, Nobuhiko -- Phung, Qui -- Chan, Salina -- Chaudhari, Ruchir -- Quan, Casey -- O'Rourke, Karen M -- Eby, Michael -- Pietras, Eric -- Cheng, Genhong -- Bazan, J Fernando -- Zhang, Zemin -- Arnott, David -- Dixit, Vishva M -- New York, N.Y. -- Science. 2007 Dec 7;318(5856):1628-32. Epub 2007 Nov 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiological Chemistry, Genentech, South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17991829" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Cell Line ; Endopeptidases/*metabolism ; Humans ; Interferon Type I/*biosynthesis/genetics ; Interferon-alpha/genetics ; Molecular Sequence Data ; NF-kappa B/metabolism ; Protein Structure, Tertiary ; RNA, Small Interfering ; Signal Transduction ; TNF Receptor-Associated Factor 3/metabolism ; Toll-Like Receptor 3/metabolism ; Ubiquitin/metabolism ; Ubiquitination
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  • 45
    Publication Date: 2007-04-28
    Description: By screening N-ethyl-N-nitrosourea-mutagenized animals for alterations in rhythms of wheel-running activity, we identified a mouse mutation, after hours (Afh). The mutation, a Cys(358)Ser substitution in Fbxl3, an F-box protein with leucine-rich repeats, results in long free-running rhythms of about 27 hours in homozygotes. Circadian transcriptional and translational oscillations are attenuated in Afh mice. The Afh allele significantly affected Per2 expression and delayed the rate of Cry protein degradation in Per2::Luciferase tissue slices. Our in vivo and in vitro studies reveal a central role for Fbxl3 in mammalian circadian timekeeping.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Godinho, Sofia I H -- Maywood, Elizabeth S -- Shaw, Linda -- Tucci, Valter -- Barnard, Alun R -- Busino, Luca -- Pagano, Michele -- Kendall, Rachel -- Quwailid, Mohamed M -- Romero, M Rosario -- O'neill, John -- Chesham, Johanna E -- Brooker, Debra -- Lalanne, Zuzanna -- Hastings, Michael H -- Nolan, Patrick M -- MC_U105170643/Medical Research Council/United Kingdom -- MC_U142684172/Medical Research Council/United Kingdom -- MC_U142684173/Medical Research Council/United Kingdom -- MC_U142684175/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2007 May 11;316(5826):897-900. Epub 2007 Apr 26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council (MRC) Mammalian Genetics Unit, Harwell, Oxfordshire OX11 0RD, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17463252" target="_blank"〉PubMed〈/a〉
    Keywords: ARNTL Transcription Factors ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Basic Helix-Loop-Helix Transcription Factors/genetics/metabolism ; CLOCK Proteins ; COS Cells ; Cell Cycle Proteins/genetics/metabolism ; Cercopithecus aethiops ; *Circadian Rhythm/genetics ; Crosses, Genetic ; Cryptochromes ; F-Box Proteins/*genetics/*physiology ; Female ; Flavoproteins/genetics/metabolism ; Gene Expression Regulation ; Liver/metabolism ; Lung/metabolism ; Male ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C3H ; Molecular Sequence Data ; Nuclear Proteins/genetics/metabolism ; Period Circadian Proteins ; *Point Mutation ; Suprachiasmatic Nucleus/metabolism ; Trans-Activators/genetics/metabolism ; Transcription Factors/genetics/metabolism ; Transcription, Genetic
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  • 46
    Publication Date: 2007-03-10
    Description: Peptidoglycan glycosyltransferases (GTs) catalyze the polymerization step of cell-wall biosynthesis, are membrane-bound, and are highly conserved across all bacteria. Long considered the "holy grail" of antibiotic research, they represent an essential and easily accessible drug target for antibiotic-resistant bacteria, including methicillin-resistant Staphylococcus aureus. We have determined the 2.8 angstrom structure of a bifunctional cell-wall cross-linking enzyme, including its transpeptidase and GT domains, both unliganded and complexed with the substrate analog moenomycin. The peptidoglycan GTs adopt a fold distinct from those of other GT classes. The structures give insight into critical features of the catalytic mechanism and key interactions required for enzyme inhibition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lovering, Andrew L -- de Castro, Liza H -- Lim, Daniel -- Strynadka, Natalie C J -- New York, N.Y. -- Science. 2007 Mar 9;315(5817):1402-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, and Center for Blood Research, University of British Columbia, 2350 Health Sciences Mall, Vancouver, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17347437" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Aminoacyltransferases/*chemistry/metabolism ; Anti-Bacterial Agents/chemistry/metabolism ; Apoenzymes/chemistry ; Binding Sites ; Carbohydrate Conformation ; Carbohydrate Sequence ; Catalytic Domain ; Cell Wall/*metabolism ; Crystallography, X-Ray ; Enzyme Inhibitors/chemistry/metabolism/pharmacology ; Glycosylation ; Models, Molecular ; Molecular Sequence Data ; Multienzyme Complexes/chemistry/metabolism ; Oligosaccharides/chemistry/metabolism/pharmacology ; Penicillin-Binding Proteins/*chemistry/metabolism ; Peptidoglycan/*biosynthesis ; Peptidoglycan Glycosyltransferase/*chemistry/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Staphylococcus aureus/*enzymology/metabolism
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  • 47
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-06-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taylor, Michael W -- Thacker, Robert W -- Hentschel, Ute -- New York, N.Y. -- Science. 2007 Jun 29;316(5833):1854-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Biological Sciences, University of Auckland, Private Bag 92019, Auckland, New Zealand.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17600204" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Physiological Phenomena ; *Biological Evolution ; Calcification, Physiologic ; Carbonic Anhydrases/*genetics/metabolism ; Computational Biology ; Genome ; Porifera/enzymology/*genetics/*microbiology/physiology ; Silicates/metabolism ; *Symbiosis
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  • 48
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-03-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Buckling, Angus -- New York, N.Y. -- Science. 2007 Mar 2;315(5816):1227-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Oxford, Oxford OX1 3PS, UK. angus.buckling@zoology.oxford.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17332398" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacteria/growth & development/*virology ; Bacterial Physiological Phenomena ; Bacteriophages/*pathogenicity/physiology ; *Biological Evolution ; Granulovirus/*pathogenicity/physiology ; Larva/physiology/virology ; Moths/*physiology/*virology ; Movement ; Selection, Genetic ; Virus Replication
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  • 49
    Publication Date: 2007-02-03
    Description: Acetylation of histone H3 lysine 56 (H3-K56) occurs in S phase, and cells lacking H3-K56 acetylation are sensitive to DNA-damaging agents. However, the histone acetyltransferase (HAT) that catalyzes global H3-K56 acetylation has not been found. Here we show that regulation of Ty1 transposition gene product 109 (Rtt109) is an H3-K56 HAT. Cells lacking Rtt109 or expressing rtt109 mutants with alterations at a conserved aspartate residue lose H3-K56 acetylation and exhibit increased sensitivity toward genotoxic agents, as well as elevated levels of spontaneous chromosome breaks. Thus, Rtt109, which shares no sequence homology with any other known HATs, is a unique HAT that acetylates H3-K56.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Han, Junhong -- Zhou, Hui -- Horazdovsky, Bruce -- Zhang, Kangling -- Xu, Rui-Ming -- Zhang, Zhiguo -- New York, N.Y. -- Science. 2007 Feb 2;315(5812):653-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, 200 First Street SW, Rochester, MN 55905, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17272723" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Amino Acid Sequence ; Camptothecin/pharmacology ; Catalytic Domain ; Chromosome Breakage ; DNA Damage ; *DNA Replication ; Histone Acetyltransferases/chemistry/genetics/*metabolism ; Histones/*metabolism ; Hydroxyurea/pharmacology ; Lysine/*metabolism ; Methyl Methanesulfonate/pharmacology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutagens/pharmacology ; Mutation ; Recombinant Proteins/metabolism ; S Phase ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/chemistry/genetics/*metabolism ; Sequence Homology, Amino Acid
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  • 50
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-08-25
    Description: YiiP is a membrane transporter that catalyzes Zn2+/H+ exchange across the inner membrane of Escherichia coli. Mammalian homologs of YiiP play critical roles in zinc homeostasis and cell signaling. Here, we report the x-ray structure of YiiP in complex with zinc at 3.8 angstrom resolution. YiiP is a homodimer held together in a parallel orientation through four Zn2+ ions at the interface of the cytoplasmic domains, whereas the two transmembrane domains swing out to yield a Y-shaped structure. In each protomer, the cytoplasmic domain adopts a metallochaperone-like protein fold; the transmembrane domain features a bundle of six transmembrane helices and a tetrahedral Zn2+ binding site located in a cavity that is open to both the membrane outer leaflet and the periplasm.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lu, Min -- Fu, Dax -- R01 GM065137/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Sep 21;317(5845):1746-8. Epub 2007 Aug 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Brookhaven National Laboratory, Upton, NY 11973, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17717154" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; Escherichia coli/chemistry/metabolism ; Escherichia coli Proteins/*chemistry/metabolism ; Membrane Transport Proteins/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Sequence Alignment ; Zinc/*chemistry/metabolism
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  • 51
    Publication Date: 2007-09-18
    Description: Membrane attack is important for mammalian immune defense against invading microorganisms and infected host cells. Proteins of the complement membrane attack complex (MAC) and the protein perforin share a common MACPF domain that is responsible for membrane insertion and pore formation. We determined the crystal structure of the MACPF domain of complement component C8alpha at 2.5 angstrom resolution and show that it is structurally homologous to the bacterial, pore-forming, cholesterol-dependent cytolysins. The structure displays two regions that (in the bacterial cytolysins) refold into transmembrane beta hairpins, forming the lining of a barrel pore. Local hydrophobicity explains why C8alpha is the first complement protein to insert into the membrane. The size of the MACPF domain is consistent with known C9 pore sizes. These data imply that these mammalian and bacterial cytolytic proteins share a common mechanism of membrane insertion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hadders, Michael A -- Beringer, Dennis X -- Gros, Piet -- New York, N.Y. -- Science. 2007 Sep 14;317(5844):1552-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Crystal and Structural Chemistry, Bijvoet Center for Biomolecular Research, Department of Chemistry, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17872444" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Membrane/immunology/metabolism ; Complement C8/*chemistry/immunology/*metabolism ; Complement Membrane Attack Complex/*chemistry/immunology/*metabolism ; Crystallography, X-Ray ; Cytotoxins/chemistry/metabolism ; Humans ; Hydrophobic and Hydrophilic Interactions ; Membrane Glycoproteins/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Perforin ; Pore Forming Cytotoxic Proteins/chemistry/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; *Protein Structure, Tertiary
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  • 52
    Publication Date: 2007-06-02
    Description: Human bipedalism is commonly thought to have evolved from a quadrupedal terrestrial precursor, yet some recent paleontological evidence suggests that adaptations for bipedalism arose in an arboreal context. However, the adaptive benefit of arboreal bipedalism has been unknown. Here we show that it allows the most arboreal great ape, the orangutan, to access supports too flexible to be negotiated otherwise. Orangutans react to branch flexibility like humans running on springy tracks, by increasing knee and hip extension, whereas all other primatesdothe reverse. Human bipedalism is thus less an innovation than an exploitation of a locomotor behavior retained from the common great ape ancestor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thorpe, S K S -- Holder, R L -- Crompton, R H -- New York, N.Y. -- Science. 2007 Jun 1;316(5829):1328-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17540902" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Animals ; *Biological Evolution ; Biomechanical Phenomena ; Ecosystem ; Hand/anatomy & histology/physiology ; Hindlimb/anatomy & histology/physiology ; Hominidae/*anatomy & histology/*physiology ; Humans ; *Locomotion ; Pongo pygmaeus/anatomy & histology/*physiology ; Posture ; *Trees ; *Walking
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  • 53
    Publication Date: 2007-04-07
    Description: The carbon skeletons of over 55,000 naturally occurring isoprenoid compounds are constructed from four fundamental coupling reactions: chain elongation, cyclopropanation, branching, and cyclobutanation. Enzymes that catalyze chain elongation and cyclopropanation are well studied, whereas those that catalyze branching and cyclobutanation are unknown. We have catalyzed the four reactions with chimeric proteins generated by replacing segments of a chain-elongation enzyme with corresponding sequences from a cyclopropanation enzyme. Stereochemical and mechanistic considerations suggest that the four coupling enzymes could have evolved from a common ancestor through relatively small changes in the catalytic site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thulasiram, Hirekodathakallu V -- Erickson, Hans K -- Poulter, C Dale -- GM 21328/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Apr 6;316(5821):73-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Utah, 315 South 1400 East, Room 2020, Salt Lake City, UT 84112, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17412950" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Artemisia/enzymology ; Catalysis ; Catalytic Domain ; Chrysanthemum cinerariifolium/enzymology ; Cyclopropanes/chemistry ; Evolution, Molecular ; Geranyltranstransferase/chemistry/genetics/*metabolism ; Kinetics ; Molecular Conformation ; Molecular Sequence Data ; Molecular Structure ; Mutagenesis, Site-Directed ; Recombinant Fusion Proteins/chemistry/metabolism ; Stereoisomerism ; Terpenes/chemistry/*metabolism
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  • 54
    Publication Date: 2007-09-01
    Description: Cell-cell contacts are fundamental to multicellular organisms and are subject to exquisite levels of control. Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes. Here we describe a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions. Cell surface expression of deletion constructs induces intercellular spacings that correlate with the ectodomain length. These data suggest that the RPTPmu ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aricescu, A Radu -- Siebold, Christian -- Choudhuri, Kaushik -- Chang, Veronica T -- Lu, Weixian -- Davis, Simon J -- van der Merwe, P Anton -- Jones, E Yvonne -- 081894/Wellcome Trust/United Kingdom -- G9722488/Medical Research Council/United Kingdom -- G9900061/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2007 Aug 31;317(5842):1217-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research UK Receptor Structure Research Group, University of Oxford, Henry Wellcome Building of Genomic Medicine, Division of Structural Biology, Roosevelt Drive, Oxford OX3 7BN, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17761881" target="_blank"〉PubMed〈/a〉
    Keywords: Adherens Junctions/chemistry/*physiology/ultrastructure ; Amino Acid Sequence ; Cell Adhesion ; Cell Adhesion Molecules/*chemistry/metabolism ; Cell Membrane/chemistry/enzymology ; Conserved Sequence ; Dimerization ; Fibronectins/chemistry ; Humans ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; Immunoglobulins/chemistry ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Protein Structure, Tertiary ; Protein Tyrosine Phosphatases/*chemistry/genetics/*metabolism ; Receptor-Like Protein Tyrosine Phosphatases, Class 2
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  • 55
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-10-20
    Description: Arginine methylation occurs on a number of proteins involved in a variety of cellular functions. Histone tails are known to be mono- and dimethylated on multiple arginine residues where they influence chromatin remodeling and gene expression. To date, no enzyme has been shown to reverse these regulatory modifications. We demonstrate that the Jumonji domain-containing 6 protein (JMJD6) is a JmjC-containing iron- and 2-oxoglutarate-dependent dioxygenase that demethylates histone H3 at arginine 2 (H3R2) and histone H4 at arginine 3 (H4R3) in both biochemical and cell-based assays. These findings may help explain the many developmental defects observed in the JMJD6(-/-) knockout mice.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, Bingsheng -- Chen, Yue -- Zhao, Yingming -- Bruick, Richard K -- C06-RR15437-01/RR/NCRR NIH HHS/ -- CA107943/CA/NCI NIH HHS/ -- CA115962/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2007 Oct 19;318(5849):444-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9038, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17947579" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arginine/*metabolism ; HeLa Cells ; Histones/*metabolism ; Humans ; Jumonji Domain-Containing Histone Demethylases ; Methylation ; Molecular Sequence Data ; Oxidation-Reduction ; Protein Processing, Post-Translational ; Receptors, Cell Surface/chemistry/genetics/*metabolism ; Recombinant Proteins/metabolism ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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  • 56
    Publication Date: 2007-05-26
    Description: Mutations in the breast cancer susceptibility gene 1 (BRCA1) are associated with an increased risk of breast and ovarian cancers. BRCA1 participates in the cellular DNA damage response. We report the identification of receptor-associated protein 80 (RAP80) as a BRCA1-interacting protein in humans. RAP80 contains a tandem ubiquitin-interacting motif domain, which is required for its binding with ubiquitin in vitro and its damage-induced foci formation in vivo. Moreover, RAP80 specifically recruits BRCA1 to DNA damage sites and functions with BRCA1 in G2/M checkpoint control. Together, these results suggest the existence of a ubiquitination-dependent signaling pathway involved in the DNA damage response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, Hongtae -- Chen, Junjie -- Yu, Xiaochun -- R01CA089239/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2007 May 25;316(5828):1202-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Therapeutic Radiology, Yale University School of Medicine, Post Office Box 208040, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17525342" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; BRCA1 Protein/*metabolism ; Carrier Proteins/*metabolism ; Cell Cycle ; Cell Line, Tumor ; DNA/*metabolism/radiation effects ; *DNA Damage ; DNA Repair/*physiology ; HeLa Cells ; Humans ; Molecular Sequence Data ; Nuclear Proteins/*metabolism ; Protein Binding ; Protein Structure, Tertiary ; RNA, Small Interfering ; Radiation, Ionizing ; Ubiquitin/*metabolism
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  • 57
    Publication Date: 2007-09-22
    Description: Whether the Late Pleistocene hominin fossils from Flores, Indonesia, represent a new species, Homo floresiensis, or pathological modern humans has been debated. Analysis of three wrist bones from the holotype specimen (LB1) shows that it retains wrist morphology that is primitive for the African ape-human clade. In contrast, Neandertals and modern humans share derived wrist morphology that forms during embryogenesis, which diminishes the probability that pathology could result in the normal primitive state. This evidence indicates that LB1 is not a modern human with an undiagnosed pathology or growth defect; rather, it represents a species descended from a hominin ancestor that branched off before the origin of the clade that includes modern humans, Neandertals, and their last common ancestor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tocheri, Matthew W -- Orr, Caley M -- Larson, Susan G -- Sutikna, Thomas -- Jatmiko -- Saptomo, E Wahyu -- Due, Rokus Awe -- Djubiantono, Tony -- Morwood, Michael J -- Jungers, William L -- New York, N.Y. -- Science. 2007 Sep 21;317(5845):1743-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Human Origins Program, Department of Anthropology, National Museum of Natural History, Smithsonian Institution, Washington, DC 20013, USA. tocherim@si.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17885135" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Carpal Bones/anatomy & histology ; *Fossils ; Hominidae/*anatomy & histology/classification ; Humans ; Indonesia ; Wrist/*anatomy & histology
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  • 58
    Publication Date: 2007-02-03
    Description: Dimethyl sulfide (DMS) is a key compound in global sulfur and carbon cycles. DMS oxidation products cause cloud nucleation and may affect weather and climate. DMS is generated largely by bacterial catabolism of dimethylsulfoniopropionate (DMSP), a secondary metabolite made by marine algae. We demonstrate that the bacterial gene dddD is required for this process and that its transcription is induced by the DMSP substrate. Cloned dddD from the marine bacterium Marinomonas and from two bacterial strains that associate with higher plants, the N(2)-fixing symbiont Rhizobium NGR234 and the root-colonizing Burkholderia cepacia AMMD, conferred to Escherichia coli the ability to make DMS from DMSP. The inferred enzymatic mechanism for DMS liberation involves an initial step in which DMSP is modified by addition of acyl coenzyme A, rather than the immediate release of DMS by a DMSP lyase, the previously suggested mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Todd, Jonathan D -- Rogers, Rachel -- Li, You Guo -- Wexler, Margaret -- Bond, Philip L -- Sun, Lei -- Curson, Andrew R J -- Malin, Gill -- Steinke, Michael -- Johnston, Andrew W B -- New York, N.Y. -- Science. 2007 Feb 2;315(5812):666-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Biological Sciences, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17272727" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/genetics/*metabolism ; Burkholderia cepacia/genetics/growth & development/metabolism ; Cloning, Molecular ; Coenzyme A-Transferases/genetics/*metabolism ; DNA Transposable Elements ; Escherichia coli/genetics/metabolism ; *Genes, Bacterial ; *Genes, Regulator ; Marinomonas/*genetics/growth & development/*metabolism ; Molecular Sequence Data ; Operon ; Oxidation-Reduction ; Phenotype ; Poaceae/microbiology ; Promoter Regions, Genetic ; Rhizobium/genetics/growth & development/metabolism ; Sulfides/*metabolism ; Sulfonium Compounds/metabolism ; Transformation, Bacterial
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  • 59
    Publication Date: 2007-06-30
    Description: HIV-1 integrates into the host chromosome and persists as a provirus flanked by long terminal repeats (LTRs). To date, treatment regimens primarily target the virus enzymes or virus-cell fusion, but not the integrated provirus. We report here the substrate-linked protein evolution of a tailored recombinase that recognizes an asymmetric sequence within an HIV-1 LTR. This evolved recombinase efficiently excised integrated HIV proviral DNA from the genome of infected cells. Although a long way from use in the clinic, we speculate that this type of technology might be adapted in future antiretroviral therapies, among other possible uses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sarkar, Indrani -- Hauber, Ilona -- Hauber, Joachim -- Buchholz, Frank -- New York, N.Y. -- Science. 2007 Jun 29;316(5833):1912-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institute for Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, D-01307 Dresden, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17600219" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA Shuffling ; DNA, Viral/*metabolism ; *Directed Molecular Evolution ; Escherichia coli/genetics ; Gene Library ; Genome, Human ; *HIV Long Terminal Repeat ; HIV-1/*metabolism ; HeLa Cells ; Humans ; Integrases/*genetics/*metabolism ; Molecular Sequence Data ; Mutation ; Proviruses/metabolism ; Recombination, Genetic ; *Virus Integration
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  • 60
    Publication Date: 2007-09-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Asara, John M -- Garavelli, John S -- Slatter, David A -- Schweitzer, Mary H -- Freimark, Lisa M -- Phillips, Matthew -- Cantley, Lewis C -- New York, N.Y. -- Science. 2007 Sep 7;317(5843):1324-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17823333" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bone and Bones/chemistry ; Collagen/*chemistry ; *Dinosaurs ; *Elephants ; *Fossils ; Glycine/chemistry ; Mass Spectrometry ; Molecular Sequence Data ; Proline/chemistry ; Tandem Mass Spectrometry
    Print ISSN: 0036-8075
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  • 61
    Publication Date: 2007-04-14
    Description: Fossilized bones from extinct taxa harbor the potential for obtaining protein or DNA sequences that could reveal evolutionary links to extant species. We used mass spectrometry to obtain protein sequences from bones of a 160,000- to 600,000-year-old extinct mastodon (Mammut americanum) and a 68-million-year-old dinosaur (Tyrannosaurus rex). The presence of T. rex sequences indicates that their peptide bonds were remarkably stable. Mass spectrometry can thus be used to determine unique sequences from ancient organisms from peptide fragmentation patterns, a valuable tool to study the evolution and adaptation of ancient taxa from which genomic sequences are unlikely to be obtained.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Asara, John M -- Schweitzer, Mary H -- Freimark, Lisa M -- Phillips, Matthew -- Cantley, Lewis C -- New York, N.Y. -- Science. 2007 Apr 13;316(5822):280-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Signal Transduction, Beth Israel Deaconess Medical Center, Boston, MA 02115, USA. jasara@bidmc.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17431180" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bone and Bones/*chemistry ; Collagen/chemistry ; *Dinosaurs ; *Elephants ; Evolution, Molecular ; *Fossils ; Humans ; *Mass Spectrometry ; Molecular Sequence Data ; Proteins/analysis/*chemistry ; Reptilian Proteins/analysis/*chemistry ; Sequence Alignment ; Sequence Analysis, Protein ; Struthioniformes
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  • 62
    Publication Date: 2007-08-19
    Description: Integral beta-barrel proteins are found in the outer membranes of mitochondria, chloroplasts, and Gram-negative bacteria. The machine that assembles these proteins contains an integral membrane protein, called YaeT in Escherichia coli, which has one or more polypeptide transport-associated (POTRA) domains. The crystal structure of a periplasmic fragment of YaeT reveals the POTRA domain fold and suggests a model for how POTRA domains can bind different peptide sequences, as required for a machine that handles numerous beta-barrel protein precursors. Analysis of POTRA domain deletions shows which are essential and provides a view of the spatial organization of this assembly machine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, Seokhee -- Malinverni, Juliana C -- Sliz, Piotr -- Silhavy, Thomas J -- Harrison, Stephen C -- Kahne, Daniel -- GM34821/GM/NIGMS NIH HHS/ -- GM66174/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Aug 17;317(5840):961-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17702946" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Outer Membrane Proteins/*chemistry/genetics/*metabolism ; Cell Membrane/metabolism ; Crystallography, X-Ray ; Dimerization ; Escherichia coli/*chemistry/*metabolism ; Escherichia coli Proteins/*chemistry/genetics/*metabolism ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Lipoproteins/chemistry/metabolism ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Transport
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  • 63
    Publication Date: 2007-04-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martin, William -- Dagan, Tal -- Koonin, Eugene V -- Dipippo, Jonathan L -- Gogarten, J Peter -- Lake, James A -- New York, N.Y. -- Science. 2007 Apr 27;316(5824):542-3; author reply 542-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17463271" target="_blank"〉PubMed〈/a〉
    Keywords: Archaeal Proteins/chemistry ; Bacterial Proteins/chemistry ; *Biological Evolution ; *Eukaryotic Cells ; Evolution, Molecular ; Fungal Proteins/chemistry ; Genomics ; Humans ; Mitochondria ; Phagocytosis ; Prokaryotic Cells ; Proteins/*chemistry
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  • 64
    Publication Date: 2007-09-01
    Description: The faithful duplication of genetic material depends on essential DNA replication initiation factors. Cellular initiators form higher-order assemblies on replication origins, using adenosine triphosphate (ATP) to locally remodel duplex DNA and facilitate proper loading of synthetic replisomal components. To better understand initiator function, we determined the 3.4 angstrom-resolution structure of an archaeal Cdc6/Orc1 heterodimer bound to origin DNA. The structure demonstrates that, in addition to conventional DNA binding elements, initiators use their AAA+ ATPase domains to recognize origin DNA. Together these interactions establish the polarity of initiator assembly on the origin and induce substantial distortions into origin DNA strands. Biochemical and comparative analyses indicate that AAA+/DNA contacts observed in the structure are dynamic and evolutionarily conserved, suggesting that the complex forms a core component of the basal initiation machinery.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dueber, Erin L Cunningham -- Corn, Jacob E -- Bell, Stephen D -- Berger, James M -- GM071747/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Aug 31;317(5842):1210-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Miller Institute for Basic Research in Science, 2536 Channing Way 5190, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17761879" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/chemistry ; Amino Acid Sequence ; Archaeal Proteins/*chemistry/metabolism ; Binding Sites ; Conserved Sequence ; Crystallography, X-Ray ; DNA, Archaeal/*chemistry/metabolism ; DNA, Single-Stranded/chemistry/metabolism ; Dimerization ; Helix-Turn-Helix Motifs ; Models, Molecular ; Nucleic Acid Conformation ; Origin Recognition Complex/*chemistry/metabolism ; Protein Structure, Secondary ; Protein Structure, Tertiary ; *Replication Origin ; Sulfolobus solfataricus/*chemistry/metabolism
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  • 65
    Publication Date: 2007-09-29
    Description: The presence of workers that forgo reproduction and care for their siblings is a defining feature of eusociality and a major challenge for evolutionary theory. It has been proposed that worker behavior evolved from maternal care behavior. We explored this idea by studying gene expression in the primitively eusocial wasp Polistes metricus. Because little genomic information existed for this species, we used 454 sequencing to generate 391,157 brain complementary DNA reads, resulting in robust hits to 3017 genes from the honey bee genome, from which we identified and assayed orthologs of 32 honey bee behaviorally related genes. Wasp brain gene expression in workers was more similar to that in foundresses, which show maternal care, than to that in queens and gynes, which do not. Insulin-related genes were among the differentially regulated genes, suggesting that the evolution of eusociality involved major nutritional and reproductive pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Toth, Amy L -- Varala, Kranthi -- Newman, Thomas C -- Miguez, Fernando E -- Hutchison, Stephen K -- Willoughby, David A -- Simons, Jan Fredrik -- Egholm, Michael -- Hunt, James H -- Hudson, Matthew E -- Robinson, Gene E -- New York, N.Y. -- Science. 2007 Oct 19;318(5849):441-4. Epub 2007 Sep 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Entomology and Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA. amytoth@uiuc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17901299" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bees/genetics ; *Biological Evolution ; Brain/metabolism ; Female ; *Gene Expression ; Gene Expression Regulation ; *Genes, Insect ; Insect Proteins/genetics/physiology ; *Maternal Behavior ; Models, Animal ; Reproduction ; *Social Behavior ; Wasps/*genetics/metabolism/physiology
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  • 66
    Publication Date: 2007-09-08
    Description: Humans have many cognitive skills not possessed by their nearest primate relatives. The cultural intelligence hypothesis argues that this is mainly due to a species-specific set of social-cognitive skills, emerging early in ontogeny, for participating and exchanging knowledge in cultural groups. We tested this hypothesis by giving a comprehensive battery of cognitive tests to large numbers of two of humans' closest primate relatives, chimpanzees and orangutans, as well as to 2.5-year-old human children before literacy and schooling. Supporting the cultural intelligence hypothesis and contradicting the hypothesis that humans simply have more "general intelligence," we found that the children and chimpanzees had very similar cognitive skills for dealing with the physical world but that the children had more sophisticated cognitive skills than either of the ape species for dealing with the social world.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herrmann, Esther -- Call, Josep -- Hernandez-Lloreda, Maraa Victoria -- Hare, Brian -- Tomasello, Michael -- New York, N.Y. -- Science. 2007 Sep 7;317(5843):1360-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute for Evolutionary Anthropology, Leipzig, D-04103, Germany. eherrman@eva.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17823346" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Child Development/physiology ; Child, Preschool ; *Cognition ; Cultural Evolution ; *Culture ; Female ; Humans ; Intelligence Tests ; Male ; Organ Size ; Pan troglodytes/*physiology ; Pongo pygmaeus/*physiology ; Species Specificity
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  • 67
    Publication Date: 2007-02-10
    Description: The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Here, we report crystal structures at 2.9 and 2.6 A resolution for ATP- and AMP-bound forms of a core alphabetagamma adenylate-binding domain from the fission yeast AMPK homolog. ATP and AMP bind competitively to a single site in the gamma subunit, with their respective phosphate groups positioned near function-impairing mutants. Unexpectedly, ATP binds without counterions, amplifying its electrostatic effects on a critical regulatory region where all three subunits converge.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Townley, Robert -- Shapiro, Lawrence -- New York, N.Y. -- Science. 2007 Mar 23;315(5819):1726-9. Epub 2007 Feb 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17289942" target="_blank"〉PubMed〈/a〉
    Keywords: AMP-Activated Protein Kinases ; Adenosine Monophosphate/metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Binding Sites ; Binding, Competitive ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Molecular Sequence Data ; Multienzyme Complexes/*chemistry/metabolism ; Protein Kinases/*chemistry/metabolism ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism ; Protein-Serine-Threonine Kinases/*chemistry/metabolism ; Schizosaccharomyces/*enzymology
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  • 68
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-09-08
    Description: The evolution of unusually large brains in some groups of animals, notably primates, has long been a puzzle. Although early explanations tended to emphasize the brain's role in sensory or technical competence (foraging skills, innovations, and way-finding), the balance of evidence now clearly favors the suggestion that it was the computational demands of living in large, complex societies that selected for large brains. However, recent analyses suggest that it may have been the particular demands of the more intense forms of pairbonding that was the critical factor that triggered this evolutionary development. This may explain why primate sociality seems to be so different from that found in most other birds and mammals: Primate sociality is based on bonded relationships of a kind that are found only in pairbonds in other taxa.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dunbar, R I M -- Shultz, Susanne -- New York, N.Y. -- Science. 2007 Sep 7;317(5843):1344-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉British Academy Centenary Research Project, School of Biological Sciences, University of Liverpool, Liverpool L69 7ZB, UK. rimd@liverpool.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17823343" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Birds ; Brain/*physiology ; Humans ; Interpersonal Relations ; Mammals ; Organ Size ; Pair Bond ; Primates/*physiology ; *Social Behavior
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  • 69
    Publication Date: 2007-10-06
    Description: Telomeres, the DNA-protein complexes located at the end of linear eukaryotic chromosomes, are essential for chromosome stability. Until now, telomeres have been considered to be transcriptionally silent. We demonstrate that mammalian telomeres are transcribed into telomeric repeat-containing RNA (TERRA). TERRA molecules are heterogeneous in length, are transcribed from several subtelomeric loci toward chromosome ends, and localize to telomeres. We also show that suppressors with morphogenetic defects in genitalia (SMG) proteins, which are effectors of nonsense-mediated messenger RNA decay, are enriched at telomeres in vivo, negatively regulate TERRA association with chromatin, and protect chromosome ends from telomere loss. Thus, telomeres are actively transcribed into TERRA, and SMG factors represent a molecular link between TERRA regulation and the maintenance of telomere integrity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Azzalin, Claus M -- Reichenbach, Patrick -- Khoriauli, Lela -- Giulotto, Elena -- Lingner, Joachim -- New York, N.Y. -- Science. 2007 Nov 2;318(5851):798-801. Epub 2007 Oct 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Swiss Institute for Experimental Cancer Research (ISREC), CH-1066 Epalinges, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17916692" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Blotting, Northern ; Cells, Cultured ; Chromosomes, Human ; Chromosomes, Mammalian ; HeLa Cells ; Humans ; In Situ Hybridization, Fluorescence ; Mice ; Molecular Sequence Data ; Proteins/metabolism ; RNA/*genetics ; Repetitive Sequences, Nucleic Acid ; Telomerase/physiology ; Telomere/*genetics ; Transcription, Genetic ; Tumor Cells, Cultured
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  • 70
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-04-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Travis, John -- New York, N.Y. -- Science. 2007 Apr 20;316(5823):390-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17446384" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Cell Differentiation ; Developmental Biology ; Embryo, Nonmammalian/cytology/physiology ; Embryonic Development ; Epigenesis, Genetic ; Female ; Gene Expression ; *Germ Cells/cytology/physiology ; Male ; Ovum/cytology ; *Reproduction ; Spermatozoa/cytology ; Stem Cells/cytology/physiology
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  • 71
    Publication Date: 2007
    Description: After amputation, freshwater planarians properly regenerate a head or tail from the resulting anterior or posterior wound. The mechanisms that differentiate anterior from posterior and direct the replacement of the appropriate missing body parts are unknown. We found that in the planarian Schmidtea mediterranea, RNA interference (RNAi) of beta-catenin or dishevelled causes the inappropriate regeneration of a head instead of a tail at posterior amputations. Conversely, RNAi of the beta-catenin antagonist adenomatous polyposis coli results in the regeneration of a tail at anterior wounds. In addition, the silencing of beta-catenin is sufficient to transform the tail of uncut adult animals into a head. We suggest that beta-catenin functions as a molecular switch to specify and maintain anteroposterior identity during regeneration and homeostasis in planarians.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2755502/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2755502/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gurley, Kyle A -- Rink, Jochen C -- Sanchez Alvarado, Alejandro -- F32GM082016/GM/NIGMS NIH HHS/ -- R0-1 GM57260/GM/NIGMS NIH HHS/ -- R01 GM057260/GM/NIGMS NIH HHS/ -- R01 GM057260-08/GM/NIGMS NIH HHS/ -- T32CA093247/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2008 Jan 18;319(5861):323-7. Epub 2007 Dec 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology and Anatomy, Howard Hughes Medical Institute, University of Utah School of Medicine, 401 MREB, 20N 1900E, Salt Lake City, UT 84132, USA. sanchez@neuro.utah.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18063757" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/chemistry/genetics/physiology ; Adenomatous Polyposis Coli Protein/chemistry/physiology ; Amino Acid Sequence ; Animals ; Body Patterning ; Gene Expression Profiling ; Genes, APC ; Head ; Helminth Proteins/chemistry/genetics/physiology ; Homeostasis ; Molecular Sequence Data ; Phosphoproteins/chemistry/genetics/physiology ; Planarians/genetics/*physiology ; RNA Interference ; *Regeneration ; Signal Transduction ; Tail ; beta Catenin/chemistry/genetics/*physiology
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  • 72
    Publication Date: 2007
    Description: We report the draft genome sequence of the model moss Physcomitrella patens and compare its features with those of flowering plants, from which it is separated by more than 400 million years, and unicellular aquatic algae. This comparison reveals genomic changes concomitant with the evolutionary movement to land, including a general increase in gene family complexity; loss of genes associated with aquatic environments (e.g., flagellar arms); acquisition of genes for tolerating terrestrial stresses (e.g., variation in temperature and water availability); and the development of the auxin and abscisic acid signaling pathways for coordinating multicellular growth and dehydration response. The Physcomitrella genome provides a resource for phylogenetic inferences about gene function and for experimental analysis of plant processes through this plant's unique facility for reverse genetics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rensing, Stefan A -- Lang, Daniel -- Zimmer, Andreas D -- Terry, Astrid -- Salamov, Asaf -- Shapiro, Harris -- Nishiyama, Tomoaki -- Perroud, Pierre-Francois -- Lindquist, Erika A -- Kamisugi, Yasuko -- Tanahashi, Takako -- Sakakibara, Keiko -- Fujita, Tomomichi -- Oishi, Kazuko -- Shin-I, Tadasu -- Kuroki, Yoko -- Toyoda, Atsushi -- Suzuki, Yutaka -- Hashimoto, Shin-Ichi -- Yamaguchi, Kazuo -- Sugano, Sumio -- Kohara, Yuji -- Fujiyama, Asao -- Anterola, Aldwin -- Aoki, Setsuyuki -- Ashton, Neil -- Barbazuk, W Brad -- Barker, Elizabeth -- Bennetzen, Jeffrey L -- Blankenship, Robert -- Cho, Sung Hyun -- Dutcher, Susan K -- Estelle, Mark -- Fawcett, Jeffrey A -- Gundlach, Heidrun -- Hanada, Kousuke -- Heyl, Alexander -- Hicks, Karen A -- Hughes, Jon -- Lohr, Martin -- Mayer, Klaus -- Melkozernov, Alexander -- Murata, Takashi -- Nelson, David R -- Pils, Birgit -- Prigge, Michael -- Reiss, Bernd -- Renner, Tanya -- Rombauts, Stephane -- Rushton, Paul J -- Sanderfoot, Anton -- Schween, Gabriele -- Shiu, Shin-Han -- Stueber, Kurt -- Theodoulou, Frederica L -- Tu, Hank -- Van de Peer, Yves -- Verrier, Paul J -- Waters, Elizabeth -- Wood, Andrew -- Yang, Lixing -- Cove, David -- Cuming, Andrew C -- Hasebe, Mitsuyasu -- Lucas, Susan -- Mishler, Brent D -- Reski, Ralf -- Grigoriev, Igor V -- Quatrano, Ralph S -- Boore, Jeffrey L -- BBS/E/C/00004948/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2008 Jan 4;319(5859):64-9. Epub 2007 Dec 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Plant Biotechnology, Faculty of Biology, University of Freiburg, Schaenzlestrasse 1, D-79104 Freiburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18079367" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Angiosperms/genetics/physiology ; Animals ; Arabidopsis/genetics/physiology ; *Biological Evolution ; Bryopsida/*genetics/physiology ; Chlamydomonas reinhardtii/genetics/physiology ; Computational Biology ; DNA Repair ; Dehydration ; Gene Duplication ; Genes, Plant ; *Genome, Plant ; Metabolic Networks and Pathways/genetics ; Multigene Family ; Oryza/genetics/physiology ; Phylogeny ; Plant Proteins/genetics/physiology ; Repetitive Sequences, Nucleic Acid ; Retroelements ; Sequence Analysis, DNA ; Signal Transduction/genetics
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  • 73
    Publication Date: 2007-12-15
    Description: PIK3CA, one of the two most frequently mutated oncogenes in human tumors, codes for p110alpha, the catalytic subunit of a phosphatidylinositol 3-kinase, isoform alpha (PI3Kalpha, p110alpha/p85). Here, we report a 3.0 angstrom resolution structure of a complex between p110alpha and a polypeptide containing the p110alpha-binding domains of p85alpha, a protein required for its enzymatic activity. The structure shows that many of the mutations occur at residues lying at the interfaces between p110alpha and p85alpha or between the kinase domain of p110alpha and other domains within the catalytic subunit. Disruptions of these interactions are likely to affect the regulation of kinase activity by p85 or the catalytic activity of the enzyme, respectively. In addition to providing new insights about the structure of PI3Kalpha, these results suggest specific mechanisms for the effect of oncogenic mutations in p110alpha and p85alpha.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Chuan-Hsiang -- Mandelker, Diana -- Schmidt-Kittler, Oleg -- Samuels, Yardena -- Velculescu, Victor E -- Kinzler, Kenneth W -- Vogelstein, Bert -- Gabelli, Sandra B -- Amzel, L Mario -- CA 43460/CA/NCI NIH HHS/ -- GM 07184/GM/NIGMS NIH HHS/ -- GM066895/GM/NIGMS NIH HHS/ -- GM07309/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Dec 14;318(5857):1744-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18079394" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate ; Amino Acid Sequence ; Binding Sites ; Catalytic Domain ; Crystallography, X-Ray ; Humans ; Models, Molecular ; Molecular Sequence Data ; *Mutation ; Neoplasms/*genetics ; Phosphatidylinositol 3-Kinases/*chemistry/genetics/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry/genetics/metabolism ; src Homology Domains
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  • 74
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-01-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mazur, Allan -- New York, N.Y. -- Science. 2007 Jan 12;315(5809):187.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17218507" target="_blank"〉PubMed〈/a〉
    Keywords: Attitude ; *Biological Evolution ; Educational Status ; Humans ; *Politics ; Religion ; United States
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  • 75
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-03-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balter, Michael -- New York, N.Y. -- Science. 2007 Mar 2;315(5816):1208-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17332386" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Astrocytes/physiology ; *Biological Evolution ; Brain/anatomy & histology/*cytology/*physiology ; Cell Shape ; Hominidae/anatomy & histology ; Humans ; Neural Pathways ; Neurons/*cytology/*physiology ; Organ Size ; Synapses/physiology ; Synaptic Transmission ; Thrombospondins/genetics/metabolism ; Whales/anatomy & histology
    Print ISSN: 0036-8075
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  • 76
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-07-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hunt, Gene -- New York, N.Y. -- Science. 2007 Jul 27;317(5837):459-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Paleobiology, National Museum of Natural History, Smithsonian Institution, Washington, DC 20013-7012. hunte@si.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17656707" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arthropods/*anatomy & histology/classification/genetics ; *Biological Evolution ; *Fossils ; Genetic Speciation ; Genetic Variation ; Paleontology ; Time
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  • 77
    Publication Date: 2007-05-26
    Description: The BRCT repeats of the breast and ovarian cancer predisposition protein BRCA1 are essential for tumor suppression. Phosphopeptide affinity proteomic analysis identified a protein, Abraxas, that directly binds the BRCA1 BRCT repeats through a phospho-Ser-X-X-Phe motif. Abraxas binds BRCA1 to the mutual exclusion of BACH1 (BRCA1-associated C-terminal helicase) and CtIP (CtBP-interacting protein), forming a third type of BRCA1 complex. Abraxas recruits the ubiquitin-interacting motif (UIM)-containing protein RAP80 to BRCA1. Both Abraxas and RAP80 were required for DNA damage resistance, G(2)-M checkpoint control, and DNA repair. RAP80 was required for optimal accumulation of BRCA1 on damaged DNA (foci) in response to ionizing radiation, and the UIM domains alone were capable of foci formation. The RAP80-Abraxas complex may help recruit BRCA1 to DNA damage sites in part through recognition of ubiquitinated proteins.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3573690/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3573690/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Bin -- Matsuoka, Shuhei -- Ballif, Bryan A -- Zhang, Dong -- Smogorzewska, Agata -- Gygi, Steven P -- Elledge, Stephen J -- 1KO1, CA116275-01/CA/NCI NIH HHS/ -- 1U19A1067751/PHS HHS/ -- T32CA09216/CA/NCI NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2007 May 25;316(5828):1194-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Center for Genetics and Genomics, Brigham and Women's Hospital, Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17525340" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; BRCA1 Protein/*physiology ; Carrier Proteins/*physiology ; Cell Line, Tumor ; *DNA Damage ; *DNA Repair ; HeLa Cells ; Humans ; Mass Spectrometry ; Molecular Sequence Data ; Nuclear Proteins/*physiology ; Protein Binding ; Protein Structure, Tertiary
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  • 78
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-08-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2007 Aug 17;317(5840):894-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17702923" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Conserved Sequence ; *DNA Transposable Elements ; Fishes/genetics ; Gene Expression Regulation, Developmental ; Humans ; *Interspersed Repetitive Sequences ; Mammals/genetics ; Short Interspersed Nucleotide Elements ; Vertebrates/genetics
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  • 79
    Publication Date: 2007-12-08
    Description: Regulated intramembrane proteolysis by members of the site-2 protease (S2P) family is an important signaling mechanism conserved from bacteria to humans. Here we report the crystal structure of the transmembrane core domain of an S2P metalloprotease from Methanocaldococcus jannaschii. The protease consists of six transmembrane segments, with the catalytic zinc atom coordinated by two histidine residues and one aspartate residue approximately 14 angstroms into the lipid membrane surface. The protease exhibits two distinct conformations in the crystals. In the closed conformation, the active site is surrounded by transmembrane helices and is impermeable to substrate peptide; water molecules gain access to zinc through a polar, central channel that opens to the cytosolic side. In the open conformation, transmembrane helices alpha1 and alpha6 separate from each other by 10 to 12 angstroms, exposing the active site to substrate entry. The structure reveals how zinc embedded in an integral membrane protein can catalyze peptide cleavage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feng, Liang -- Yan, Hanchi -- Wu, Zhuoru -- Yan, Nieng -- Wang, Zhe -- Jeffrey, Philip D -- Shi, Yigong -- New York, N.Y. -- Science. 2007 Dec 7;318(5856):1608-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Lewis Thomas Laboratory, Princeton University, Princeton, NJ 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18063795" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Archaeal Proteins/chemistry/metabolism ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Catalysis ; Catalytic Domain ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Membrane Proteins/*chemistry/metabolism ; Metalloendopeptidases/*chemistry/metabolism ; Methanococcus/*enzymology ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Water ; Zinc/chemistry
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  • 80
    Publication Date: 2007-11-17
    Description: Cells respond to DNA double-strand breaks by recruiting factors such as the DNA-damage mediator protein MDC1, the p53-binding protein 1 (53BP1), and the breast cancer susceptibility protein BRCA1 to sites of damaged DNA. Here, we reveal that the ubiquitin ligase RNF8 mediates ubiquitin conjugation and 53BP1 and BRCA1 focal accumulation at sites of DNA lesions. Moreover, we establish that MDC1 recruits RNF8 through phosphodependent interactions between the RNF8 forkhead-associated domain and motifs in MDC1 that are phosphorylated by the DNA-damage activated protein kinase ataxia telangiectasia mutated (ATM). We also show that depletion of the E2 enzyme UBC13 impairs 53BP1 recruitment to sites of damage, which suggests that it cooperates with RNF8. Finally, we reveal that RNF8 promotes the G2/M DNA damage checkpoint and resistance to ionizing radiation. These results demonstrate how the DNA-damage response is orchestrated by ATM-dependent phosphorylation of MDC1 and RNF8-mediated ubiquitination.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2430610/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2430610/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolas, Nadine K -- Chapman, J Ross -- Nakada, Shinichiro -- Ylanko, Jarkko -- Chahwan, Richard -- Sweeney, Frederic D -- Panier, Stephanie -- Mendez, Megan -- Wildenhain, Jan -- Thomson, Timothy M -- Pelletier, Laurence -- Jackson, Stephen P -- Durocher, Daniel -- A5290/Cancer Research UK/United Kingdom -- New York, N.Y. -- Science. 2007 Dec 7;318(5856):1637-40. Epub 2007 Nov 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Avenue, Toronto M5G1X5, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18006705" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Ataxia Telangiectasia Mutated Proteins ; BRCA1 Protein/metabolism ; Cell Cycle Proteins/metabolism ; Cell Line, Tumor ; Cell Nucleus Structures/*genetics ; *DNA Breaks, Double-Stranded ; DNA Repair ; DNA-Binding Proteins/chemistry/*metabolism ; HeLa Cells ; Humans ; Intracellular Signaling Peptides and Proteins/metabolism ; Molecular Sequence Data ; Nuclear Proteins/chemistry/metabolism ; Phosphorylation ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/metabolism ; RNA, Small Interfering ; Trans-Activators/chemistry/metabolism ; Tumor Suppressor Proteins/metabolism ; Ubiquitin/metabolism ; Ubiquitin-Conjugating Enzymes/metabolism ; Ubiquitin-Protein Ligases/*metabolism ; Ubiquitination
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  • 81
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-12-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McInerney, James O -- Pisani, Davide -- New York, N.Y. -- Science. 2007 Nov 30;318(5855):1390-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, National University of Ireland Maynooth, Maynooth, County Kildare, Ireland. james.o.mcinerney@nuim.ie〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18048672" target="_blank"〉PubMed〈/a〉
    Keywords: Archaea/classification/genetics ; Bacteria/classification/genetics ; *Biological Evolution ; Escherichia coli/classification/*genetics ; *Gene Transfer, Horizontal ; *Genes, Archaeal ; *Genes, Bacterial ; Genetic Speciation ; Phylogeny
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  • 82
    Publication Date: 2007-10-27
    Description: mazEF is a toxin-antitoxin module located on many bacterial chromosomes, including those of pathogens. Here, we report that Escherichia coli mazEF-mediated cell death is a population phenomenon requiring a quorum-sensing molecule that we call the extracellular death factor (EDF). Structural analysis revealed that EDF is a linear pentapeptide, Asn-Asn-Trp-Asn-Asn. Each of the five amino acids of EDF is important for its activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolodkin-Gal, Ilana -- Hazan, Ronen -- Gaathon, Ariel -- Carmeli, Shmuel -- Engelberg-Kulka, Hanna -- GM069509/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Oct 26;318(5850):652-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Hebrew University-Hadassah Medical School, Jerusalem 91120, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17962566" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Apoptosis ; Aspartate-Ammonia Ligase/genetics/metabolism ; DNA-Binding Proteins/*physiology ; Endoribonucleases/*physiology ; Escherichia coli/cytology/growth & development/*physiology ; Escherichia coli Proteins/*physiology ; Microbial Viability ; Oligopeptides/chemistry/isolation & purification/*metabolism ; *Quorum Sensing
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  • 83
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-05-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2007 May 18;316(5827):967.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17510332" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; DNA/*genetics ; DNA, Mitochondrial/genetics ; Databases, Nucleic Acid ; *Fossils ; Gene Flow ; Genome ; Genome, Human ; Hominidae/*genetics ; Humans ; *Hybridization, Genetic ; Polymorphism, Single Nucleotide ; *Sexual Behavior
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  • 84
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-02-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Enserink, Martin -- New York, N.Y. -- Science. 2007 Feb 16;315(5814):925.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17303725" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Europe ; *Religion and Science
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  • 85
    Publication Date: 2007-06-02
    Description: Sponges (phylum Porifera) were prolific reef-building organisms during the Paleozoic and Mesozoic approximately 542 to 65 million years ago. These ancient animals inherited components of the first multicellular skeletogenic toolkit from the last common ancestor of the Metazoa. Using a paleogenomics approach, including gene- and protein-expression techniques and phylogenetic reconstruction, we show that a molecular component of this toolkit was the precursor to the alpha-carbonic anhydrases (alpha-CAs), a gene family used by extant animals in a variety of fundamental physiological processes. We used the coralline demosponge Astrosclera willeyana, a "living fossil" that has survived from the Mesozoic, to provide insight into the evolution of the ability to biocalcify, and show that the alpha-CA family expanded from a single ancestral gene through several independent gene-duplication events in sponges and eumetazoans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jackson, Daniel J -- Macis, Luciana -- Reitner, Joachim -- Degnan, Bernard M -- Worheide, Gert -- New York, N.Y. -- Science. 2007 Jun 29;316(5833):1893-5. Epub 2007 May 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Geoscience Centre Gottingen, Department of Geobiology, Goldschmidtstrasse 3, D-37077 Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17540861" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Bicarbonates/metabolism ; *Calcification, Physiologic ; Calcium Carbonate/analysis/metabolism ; Carbonic Anhydrases/chemistry/*genetics/*metabolism ; Computational Biology ; Evolution, Molecular ; Gene Duplication ; Genes ; Genomics ; Molecular Sequence Data ; Porifera/anatomy & histology/enzymology/*genetics/*physiology ; Recombinant Proteins/chemistry/metabolism
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  • 86
    Publication Date: 2007-11-03
    Description: A full understanding of primate morphological and genomic evolution requires the identification of their closest living relative. In order to resolve the ancestral relationships among primates and their closest relatives, we searched multispecies genome alignments for phylogenetically informative rare genomic changes within the superordinal group Euarchonta, which includes the orders Primates, Dermoptera (colugos), and Scandentia (treeshrews). We also constructed phylogenetic trees from 14 kilobases of nuclear genes for representatives from most major primate lineages, both extant colugos, and multiple treeshrews, including the pentail treeshrew, Ptilocercus lowii, the only living member of the family Ptilocercidae. A relaxed molecular clock analysis including Ptilocercus suggests that treeshrews arose approximately 63 million years ago. Our data show that colugos are the closest living relatives of primates and indicate that their divergence occurred in the Cretaceous.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Janecka, Jan E -- Miller, Webb -- Pringle, Thomas H -- Wiens, Frank -- Zitzmann, Annette -- Helgen, Kristofer M -- Springer, Mark S -- Murphy, William J -- HG02238/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2007 Nov 2;318(5851):792-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Veterinary Integrative Biosciences, Texas A&M University, College Station, TX 77843, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17975064" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Dna ; Evolution, Molecular ; Fossils ; Genome ; Humans ; Mammals/classification/genetics ; Molecular Sequence Data ; Phylogeny ; Primates/classification/*genetics ; Scandentia/classification/genetics ; Sequence Alignment
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  • 87
    Publication Date: 2007-06-09
    Description: Root hairs and rhizoids are cells with rooting functions in land plants. We describe two basic helix-loop-helix transcription factors that control root hair development in the sporophyte (2n) of the angiosperm Arabidopsis thaliana and rhizoid development in the gametophytes (n) of the bryophyte Physcomitrella patens. The phylogeny of land plants supports the hypothesis that early land plants were bryophyte-like and possessed a dominant gametophyte and later the sporophyte rose to dominance. If this hypothesis is correct, our data suggest that the increase in morphological complexity of the sporophyte body in the Paleozoic resulted at least in part from the recruitment of regulatory genes from gametophyte to sporophyte.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Menand, Benoit -- Yi, Keke -- Jouannic, Stefan -- Hoffmann, Laurent -- Ryan, Eoin -- Linstead, Paul -- Schaefer, Didier G -- Dolan, Liam -- BBS/E/J/0000A218/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2007 Jun 8;316(5830):1477-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Developmental Biology, John Innes Centre, Norwich NR47UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17556585" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/cytology/genetics/growth & development/*physiology ; Arabidopsis Proteins/genetics/*physiology ; Basic Helix-Loop-Helix Transcription Factors/genetics/*physiology ; Biological Evolution ; Bryopsida/cytology/genetics/growth & development/*physiology ; Diploidy ; Genes, Plant ; Haploidy ; Molecular Sequence Data ; Mutation ; Phylogeny ; Plant Epidermis/cytology/physiology ; Plant Proteins/genetics/physiology ; Plant Roots/*cytology/growth & development ; Plants, Genetically Modified
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  • 88
    Publication Date: 2007-08-11
    Description: Evolution by natural selection is driven by the continuous generation of adaptive mutations. We measured the genomic mutation rate that generates beneficial mutations and their effects on fitness in Escherichia coli under conditions in which the effect of competition between lineages carrying different beneficial mutations is minimized. We found a rate on the order of 10(-5) per genome per generation, which is 1000 times as high as previous estimates, and a mean selective advantage of 1%. Such a high rate of adaptive evolution has implications for the evolution of antibiotic resistance and pathogenicity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perfeito, Lilia -- Fernandes, Lisete -- Mota, Catarina -- Gordo, Isabel -- New York, N.Y. -- Science. 2007 Aug 10;317(5839):813-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Instituto Gulbenkian de Ciencia, Rua da Quinta Grande, number 6, 2780-156 Oeiras, Portugal.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17690297" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptation, Biological ; *Biological Evolution ; Escherichia coli/*genetics/physiology ; *Genome, Bacterial ; Microsatellite Repeats ; *Mutation ; *Selection, Genetic
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  • 89
    Publication Date: 2007-11-17
    Description: Thorpe et al. (Reports, 1 June 2007, p. 1328) concluded that human bipedalism evolved from a type of bipedal posture they observed in extant orangutans with seemingly human-like extended knees. However, humans share knuckle-walking characters with African apes that are absent in orangutans. These are most parsimoniously explained by positing a knuckle-walking precursor to human bipedalism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Begun, D R -- Richmond, B G -- Strait, D S -- New York, N.Y. -- Science. 2007 Nov 16;318(5853):1066; author reply 1066.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anthropology, University of Toronto, Toronto, ON, M5S 2S2, Canada. begun@chass.utoronto.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18006725" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Animals ; *Biological Evolution ; Biomechanical Phenomena ; Hand ; Hominidae/physiology ; Humans ; Pongo pygmaeus/*physiology ; Posture ; Trees ; *Walking
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  • 90
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-02-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wheelis, Mark -- New York, N.Y. -- Science. 2007 Feb 2;315(5812):597.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17272702" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; History, 19th Century
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  • 91
    Publication Date: 2007-01-20
    Description: Cysteine (Cys) residues often play critical roles in proteins; however, identification of their specific functions has been limited to case-by-case experimental approaches. We developed a procedure for high-throughput identification of catalytic redox-active Cys in proteins by searching for sporadic selenocysteine-Cys pairs in sequence databases. This method is independent of protein family, structure, and taxon. We used it to selectively detect the majority of known proteins with redox-active Cys and to make additional predictions, one of which was verified. Rapid accumulation of sequence information from genomic and metagenomic projects should allow detection of many additional oxidoreductase families as well as identification of redox-active Cys in these proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fomenko, Dmitri E -- Xing, Weibing -- Adair, Blakely M -- Thomas, David J -- Gladyshev, Vadim N -- AG021518/AG/NIA NIH HHS/ -- GM061603/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Jan 19;315(5810):387-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17234949" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Archaeal Proteins/chemistry ; Bacterial Proteins/chemistry ; Base Sequence ; Catalysis ; Computational Biology ; Cysteine/analysis/*chemistry ; *Databases, Nucleic Acid ; *Databases, Protein ; Enzymes/*chemistry ; Eukaryotic Cells ; Evolution, Molecular ; Methyltransferases/chemistry ; Molecular Sequence Data ; Oxidation-Reduction ; Oxidoreductases/chemistry ; Proteins/*chemistry ; Selenocysteine/chemistry ; Selenoproteins/*chemistry
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  • 92
    Publication Date: 2007-11-10
    Description: Variants in the FTO (fat mass and obesity associated) gene are associated with increased body mass index in humans. Here, we show by bioinformatics analysis that FTO shares sequence motifs with Fe(II)- and 2-oxoglutarate-dependent oxygenases. We find that recombinant murine Fto catalyzes the Fe(II)- and 2OG-dependent demethylation of 3-methylthymine in single-stranded DNA, with concomitant production of succinate, formaldehyde, and carbon dioxide. Consistent with a potential role in nucleic acid demethylation, Fto localizes to the nucleus in transfected cells. Studies of wild-type mice indicate that Fto messenger RNA (mRNA) is most abundant in the brain, particularly in hypothalamic nuclei governing energy balance, and that Fto mRNA levels in the arcuate nucleus are regulated by feeding and fasting. Studies can now be directed toward determining the physiologically relevant FTO substrate and how nucleic acid methylation status is linked to increased fat mass.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2668859/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2668859/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gerken, Thomas -- Girard, Christophe A -- Tung, Yi-Chun Loraine -- Webby, Celia J -- Saudek, Vladimir -- Hewitson, Kirsty S -- Yeo, Giles S H -- McDonough, Michael A -- Cunliffe, Sharon -- McNeill, Luke A -- Galvanovskis, Juris -- Rorsman, Patrik -- Robins, Peter -- Prieur, Xavier -- Coll, Anthony P -- Ma, Marcella -- Jovanovic, Zorica -- Farooqi, I Sadaf -- Sedgwick, Barbara -- Barroso, Ines -- Lindahl, Tomas -- Ponting, Chris P -- Ashcroft, Frances M -- O'Rahilly, Stephen -- Schofield, Christopher J -- 068086/Wellcome Trust/United Kingdom -- 077016/Wellcome Trust/United Kingdom -- G108/617/Medical Research Council/United Kingdom -- G9824984/Medical Research Council/United Kingdom -- MC_U137761446/Medical Research Council/United Kingdom -- U54 GM064346/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Nov 30;318(5855):1469-72. Epub 2007 Nov 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chemistry Research Laboratory and Oxford Centre for Integrative Systems Biology, University of Oxford, 12 Mansfield Road, Oxford, Oxon OX1 3TA, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17991826" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/enzymology/metabolism ; Cell Nucleus/enzymology ; Computational Biology ; DNA/*metabolism ; DNA Methylation ; DNA, Single-Stranded/metabolism ; Eating ; Energy Metabolism ; Fasting ; Ferrous Compounds/metabolism ; Hypothalamus/enzymology/metabolism ; Ketoglutaric Acids/*metabolism ; Male ; Mice ; Mixed Function Oxygenases ; Molecular Sequence Data ; Oxo-Acid-Lyases/chemistry/*genetics/*metabolism ; RNA, Messenger/genetics/metabolism ; Recombinant Proteins/metabolism ; Succinic Acid/metabolism ; Thymine/analogs & derivatives/metabolism
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  • 93
    Publication Date: 2007-01-27
    Description: Although Whibley et al. (Reports, 18 August 2006, p. 963) argue for the presence of high-fitness ridges in the Antirrhinum floral-color adaptive landscape, their data are equally compatible with adaptive landscapes having a single peak and no ridges. Their demonstration of divergent selection across a hybrid zone argues against the presence of adaptive ridges.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rausher, Mark D -- New York, N.Y. -- Science. 2007 Jan 26;315(5811):461; author reply 461.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Duke University, Box 90338, Durham, NC 27708, USA. mrausher@duke.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17255497" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Antirrhinum/classification/*genetics ; *Biological Evolution ; Flowers/*genetics ; Genetic Speciation ; Genotype ; Hybridization, Genetic ; Phenotype ; Pigmentation/*genetics ; *Selection, Genetic
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  • 94
    Publication Date: 2007-03-31
    Description: A variety of methods exist for the design or selection of antibodies and other proteins that recognize the water-soluble regions of proteins; however, companion methods for targeting transmembrane (TM) regions are not available. Here, we describe a method for the computational design of peptides that target TM helices in a sequence-specific manner. To illustrate the method, peptides were designed that specifically recognize the TM helices of two closely related integrins (alphaIIbbeta3 and alphavbeta3) in micelles, bacterial membranes, and mammalian cells. These data show that sequence-specific recognition of helices in TM proteins can be achieved through optimization of the geometric complementarity of the target-host complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yin, Hang -- Slusky, Joanna S -- Berger, Bryan W -- Walters, Robin S -- Vilaire, Gaston -- Litvinov, Rustem I -- Lear, James D -- Caputo, Gregory A -- Bennett, Joel S -- DeGrado, William F -- 5T32 CA101968/CA/NCI NIH HHS/ -- 5T32 GM08275/GM/NIGMS NIH HHS/ -- GM54616/GM/NIGMS NIH HHS/ -- GM60610/GM/NIGMS NIH HHS/ -- HL40387/HL/NHLBI NIH HHS/ -- HL54500/HL/NHLBI NIH HHS/ -- T32 GM008275/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Mar 30;315(5820):1817-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17395823" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Amino Acid Motifs ; Amino Acid Sequence ; Blood Platelets/physiology ; Cell Membrane/*chemistry ; Databases, Protein ; Dimerization ; Escherichia coli/chemistry ; Fluorescence Resonance Energy Transfer ; Humans ; Integrin alphaVbeta3/*chemistry/metabolism ; Lipid Bilayers/chemistry ; Models, Molecular ; Molecular Sequence Data ; Optical Tweezers ; Osteopontin/metabolism ; Peptides/*chemistry/metabolism ; Platelet Adhesiveness ; Platelet Aggregation ; Platelet Glycoprotein GPIIb-IIIa Complex/*chemistry/metabolism ; *Protein Engineering ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Spectrum Analysis
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  • 95
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-08-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, Ann -- New York, N.Y. -- Science. 2007 Aug 10;317(5839):733.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17690266" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Female ; *Fossils ; *Hominidae/anatomy & histology/classification ; Humans ; Jaw/anatomy & histology ; Kenya ; Male ; Skull/anatomy & histology
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  • 96
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-12-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corden, Jeffry L -- New York, N.Y. -- Science. 2007 Dec 14;318(5857):1735-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Genetics, Johns Hopkins Medical School, Baltimore, MD 21205, USA. jcorden@jhmi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18079391" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Gene Expression Regulation ; Humans ; Mutation ; Phosphorylation ; Protein Structure, Tertiary ; RNA Polymerase II/chemistry/genetics/*metabolism ; Serine/metabolism ; Templates, Genetic ; *Transcription, Genetic
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  • 97
    Publication Date: 2007-01-27
    Description: How do integral membrane proteins evolve in size and complexity? Using the small multidrug-resistance protein EmrE from Escherichia coli as a model, we experimentally demonstrated that the evolution of membrane proteins composed of two homologous but oppositely oriented domains can occur in a small number of steps: An original dual-topology protein evolves, through a gene-duplication event, to a heterodimer formed by two oppositely oriented monomers. This simple evolutionary pathway can explain the frequent occurrence of membrane proteins with an internal pseudo-two-fold symmetry axis in the plane of the membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rapp, Mikaela -- Seppala, Susanna -- Granseth, Erik -- von Heijne, Gunnar -- New York, N.Y. -- Science. 2007 Mar 2;315(5816):1282-4. Epub 2007 Jan 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17255477" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antiporters/*chemistry/genetics ; Cell Membrane/*chemistry ; Dimerization ; Directed Molecular Evolution ; Drug Resistance, Bacterial ; Escherichia coli/*chemistry/drug effects/genetics/growth & development ; Escherichia coli Proteins/*chemistry/genetics ; Ethidium/pharmacology ; *Evolution, Molecular ; Gene Duplication ; Membrane Transport Proteins/*chemistry/genetics ; Molecular Sequence Data ; Mutation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Recombinant Fusion Proteins/chemistry/metabolism
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  • 98
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-06-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, Ann -- New York, N.Y. -- Science. 2007 Jun 15;316(5831):1558-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17569838" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Brain/*anatomy & histology/metabolism ; *Cooking ; *Diet ; Digestion ; Energy Intake ; *Energy Metabolism ; Fires ; *Hominidae/anatomy & histology/metabolism ; Humans ; Meat ; Paleodontology ; Paleontology ; Tooth/anatomy & histology
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  • 99
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-09-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keeling, Patrick J -- New York, N.Y. -- Science. 2007 Sep 28;317(5846):1875-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Botany Department, Canadian Institute for Advanced Research, University of British Columbia, Vancouver, BC, V6T 1Z4 Canada. pkeeling@interchange.ubc.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17901321" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Eukaryotic Cells ; Genes, Protozoan ; *Genome, Protozoan ; Genomics ; Giardia lamblia/classification/*genetics/physiology ; Organelles/metabolism/ultrastructure ; Phylogeny
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  • 100
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-10-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ritchie, Michael G -- New York, N.Y. -- Science. 2007 Oct 5;318(5847):54-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of St. Andrews, Fife KY16 9AJ, UK. mgr@st-andrews.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17916717" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Fathers ; Feathers ; Female ; *Genetic Linkage ; *Genetic Speciation ; Hybridization, Genetic ; Male ; *Mating Preference, Animal ; Sex Chromosomes/*genetics ; Songbirds/anatomy & histology/genetics/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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