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  • Articles  (106)
  • Latest Papers from Table of Contents or Articles in Press  (106)
  • *Biological Evolution  (58)
  • Models, Molecular  (48)
  • 2005-2009  (106)
  • 1980-1984
  • 1955-1959
  • 2007  (106)
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  • Articles  (106)
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  • Latest Papers from Table of Contents or Articles in Press  (106)
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  • 2005-2009  (106)
  • 1980-1984
  • 1955-1959
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  • 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
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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
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  • 3
    Publication Date: 2007-12-22
    Description: Protein molecules have the ability to form a rich variety of natural and artificial structures and materials. We show that amyloid fibrils, ordered supramolecular nanostructures that are self-assembled from a wide range of polypeptide molecules, have rigidities varying over four orders of magnitude, and constitute a class of high-performance biomaterials. We elucidate the molecular origin of fibril material properties and show that the major contribution to their rigidity stems from a generic interbackbone hydrogen-bonding network that is modulated by variable side-chain interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knowles, Tuomas P -- Fitzpatrick, Anthony W -- Meehan, Sarah -- Mott, Helen R -- Vendruscolo, Michele -- Dobson, Christopher M -- Welland, Mark E -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2007 Dec 21;318(5858):1900-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nanoscience Centre, University of Cambridge, J. J. Thomson Avenue, Cambridge CB3 0FF, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18096801" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloid/*chemistry ; Amyloid beta-Peptides/chemistry ; Chemistry, Physical ; Elasticity ; Humans ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Insulin/chemistry ; Lactalbumin/chemistry ; Lactoglobulins/chemistry ; Microscopy, Atomic Force ; Models, Molecular ; Muramidase/chemistry ; Nanostructures/*chemistry ; Peptide Termination Factors ; Peptides/*chemistry ; Physicochemical Phenomena ; Prealbumin/chemistry ; Prions/chemistry ; Protein Conformation ; Protein Structure, Tertiary ; Saccharomyces cerevisiae Proteins/chemistry ; Surface Tension ; alpha-Crystallin B Chain/chemistry
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  • 4
    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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  • 5
    Publication Date: 2007-04-14
    Description: The pre-B cell receptor (pre-BCR) serves as a checkpoint in B cell development. In the 2.7 angstrom structure of a human pre-BCR Fab-like fragment, consisting of an antibody heavy chain (HC) paired with the surrogate light chain, the "unique regions" of VpreB and lambda5 replace the complementarity-determining region 3 (CDR3) loop of an antibody light chain and appear to "probe" the HC CDR3, potentially influencing the selection of the antibody repertoire. Biochemical analysis indicates that the pre-BCR is impaired in its ability to recognize antigen, which, together with electron microscopic visualization of a pre-BCR dimer, suggests ligand-independent oligomerization as the likely signaling mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bankovich, Alexander J -- Raunser, Stefan -- Juo, Z Sean -- Walz, Thomas -- Davis, Mark M -- Garcia, K Christopher -- T32 AI007290/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2007 Apr 13;316(5822):291-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17431183" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Complementarity Determining Regions/chemistry/physiology ; Crystallography, X-Ray ; Humans ; Immunoglobulin Heavy Chains/chemistry/physiology ; Immunoglobulin Light Chains/chemistry/physiology ; Immunoglobulin Light Chains, Surrogate ; Membrane Glycoproteins/*chemistry/physiology/ultrastructure ; Mice ; Models, Molecular ; Pre-B Cell Receptors ; Protein Conformation ; Receptors, Antigen, B-Cell/*chemistry/physiology/ultrastructure ; Recombinant Proteins ; Structure-Activity Relationship
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  • 6
    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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  • 7
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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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  • 8
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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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  • 9
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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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  • 10
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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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  • 11
    Publication Date: 2007-08-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, Robert F -- New York, N.Y. -- Science. 2007 Aug 17;317(5840):884-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17702918" target="_blank"〉PubMed〈/a〉
    Keywords: Aldosterone/metabolism ; Animals ; Computer Simulation ; Crystallography, X-Ray ; Desoxycorticosterone/metabolism ; *Evolution, Molecular ; *Fishes ; Hydrocortisone/metabolism ; Models, Molecular ; Mutation ; Protein Conformation ; Receptors, Glucocorticoid/chemistry/*genetics/metabolism ; Receptors, Mineralocorticoid/chemistry/*genetics/metabolism ; Receptors, Steroid/chemistry/*genetics/metabolism
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  • 12
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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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  • 13
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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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  • 14
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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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  • 15
    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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  • 16
    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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  • 17
    Publication Date: 2007-12-01
    Description: How chaperone interactions affect protein folding pathways is a central problem in biology. With the use of optical tweezers and all-atom molecular dynamics simulations, we studied the effect of chaperone SecB on the folding and unfolding pathways of maltose binding protein (MBP) at the single-molecule level. In the absence of SecB, we find that the MBP polypeptide first collapses into a molten globulelike compacted state and then folds into a stable core structure onto which several alpha helices are finally wrapped. Interactions with SecB completely prevent stable tertiary contacts in the core structure but have no detectable effect on the folding of the external alpha helices. It appears that SecB only binds to the extended or molten globulelike structure and retains MBP in this latter state. Thus during MBP translocation, no energy is required to disrupt stable tertiary interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bechtluft, Philipp -- van Leeuwen, Ruud G H -- Tyreman, Matthew -- Tomkiewicz, Danuta -- Nouwen, Nico -- Tepper, Harald L -- Driessen, Arnold J M -- Tans, Sander J -- New York, N.Y. -- Science. 2007 Nov 30;318(5855):1458-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology, Groningen Bio-molecular Sciences and Biotechnology Institute and the Zernike Institute for Advanced Materials, University of Groningen, Kerklaan 30, 9751 NN Haren, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18048690" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*metabolism ; Computer Simulation ; Escherichia coli Proteins/*chemistry/metabolism ; Models, Molecular ; Optical Tweezers ; Periplasmic Binding Proteins/*chemistry/metabolism ; Protein Conformation ; *Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 18
    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
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 19
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 20
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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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  • 21
    Publication Date: 2007-04-21
    Description: We report the structures of three intermediates in the O2 activation and insertion reactions of an extradiol ring-cleaving dioxygenase. A crystal of Fe2+-containing homoprotocatechuate 2,3-dioxygenase was soaked in the slow substrate 4-nitrocatechol in a low O2 atmosphere. The x-ray crystal structure shows that three different intermediates reside in different subunits of a single homotetrameric enzyme molecule. One of these is the key substrate-alkylperoxo-Fe2+ intermediate, which has been predicted, but not structurally characterized, in an oxygenase. The intermediates define the major chemical steps of the dioxygenase mechanism and point to a general mechanistic strategy for the diverse 2-His-1-carboxylate enzyme family.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2720167/" 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/PMC2720167/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kovaleva, Elena G -- Lipscomb, John D -- GM24689/GM/NIGMS NIH HHS/ -- R01 GM024689/GM/NIGMS NIH HHS/ -- R01 GM024689-27/GM/NIGMS NIH HHS/ -- R01 GM024689-28/GM/NIGMS NIH HHS/ -- R37 GM024689/GM/NIGMS NIH HHS/ -- R37 GM024689-26/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Apr 20;316(5823):453-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17446402" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Brevibacterium/*enzymology ; Catalysis ; Catechols/chemistry/metabolism ; Crystallization ; Crystallography, X-Ray ; Dioxygenases/*chemistry/*metabolism ; Ferric Compounds/*chemistry/metabolism ; Ferrous Compounds/chemistry ; Ligands ; Models, Chemical ; Models, Molecular ; Oxygen/chemistry/metabolism ; Protein Conformation ; Protein Subunits/chemistry/metabolism ; Superoxides/chemistry
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  • 22
    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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  • 23
    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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  • 24
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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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  • 25
    Publication Date: 2007-03-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Poolman, Bert -- Geertsma, Eric R -- Slotboom, Dirk-Jan -- New York, N.Y. -- Science. 2007 Mar 2;315(5816):1229-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, and Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 4, 9747 AG Groningen, Netherlands. b.poolman@rug.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17332400" target="_blank"〉PubMed〈/a〉
    Keywords: Antiporters/*chemistry/genetics/metabolism ; Cell Membrane/*chemistry ; Dimerization ; Directed Molecular Evolution ; Escherichia coli/*chemistry ; Escherichia coli Proteins/*chemistry/genetics/metabolism ; *Evolution, Molecular ; Gene Duplication ; Membrane Proteins/*chemistry/genetics/metabolism ; Membrane Transport Proteins/*chemistry/genetics ; Models, Molecular ; Protein Folding ; Protein Structure, Tertiary ; Protein Subunits/chemistry
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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: The catalytic (C) subunit of cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) is inhibited by two classes of regulatory subunits, RI and RII. The RII subunits are substrates as well as inhibitors and do not require adenosine triphosphate (ATP) to form holoenzyme, which distinguishes them from RI subunits. To understand the molecular basis for isoform diversity, we solved the crystal structure of an RIIalpha holoenzyme and compared it to the RIalpha holoenzyme. Unphosphorylated RIIalpha(90-400), a deletion mutant, undergoes major conformational changes as both of the cAMP-binding domains wrap around the C subunit's large lobe. The hallmark of this conformational reorganization is the helix switch in domain A. The C subunit is in an open conformation, and its carboxyl-terminal tail is disordered. This structure demonstrates the conserved and isoform-specific features of RI and RII and the importance of ATP, and also provides a new paradigm for designing isoform-specific activators or antagonists for PKA.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4036697/" 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/PMC4036697/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, Jian -- Brown, Simon H J -- von Daake, Sventja -- Taylor, Susan S -- GM34921/GM/NIGMS NIH HHS/ -- R01 GM034921/GM/NIGMS NIH HHS/ -- R01 GM034921-23/GM/NIGMS NIH HHS/ -- T32-CA009524/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2007 Oct 12;318(5848):274-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17932298" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Animals ; Binding Sites ; Catalytic Domain ; Crystallography, X-Ray ; Cyclic AMP/metabolism ; Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit ; Cyclic AMP-Dependent Protein Kinase RIalpha Subunit ; Cyclic AMP-Dependent Protein Kinases/*chemistry/genetics/metabolism ; Holoenzymes/chemistry ; Hydrophobic and Hydrophilic Interactions ; Isoenzymes/chemistry ; Mice ; Models, Molecular ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary
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  • 29
    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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  • 30
    Publication Date: 2007-08-25
    Description: Biotin-dependent multifunctional enzymes carry out metabolically important carboxyl group transfer reactions and are potential targets for the treatment of obesity and type 2 diabetes. These enzymes use a tethered biotin cofactor to carry an activated carboxyl group between distantly spaced active sites. The mechanism of this transfer has remained poorly understood. Here we report the complete structure of pyruvate carboxylase at 2.0 angstroms resolution, which shows its domain arrangement. The structure, when combined with mutagenic analysis, shows that intermediate transfer occurs between active sites on separate polypeptide chains. In addition, domain rearrangements associated with activator binding decrease the distance between active-site pairs, providing a mechanism for allosteric activation. This description provides insight into the function of biotin-dependent enzymes and presents a new paradigm for multifunctional enzyme catalysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉St Maurice, Martin -- Reinhardt, Laurie -- Surinya, Kathy H -- Attwood, Paul V -- Wallace, John C -- Cleland, W Wallace -- Rayment, Ivan -- AR35186/AR/NIAMS NIH HHS/ -- GM070455/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Aug 24;317(5841):1076-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Wisconsin, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17717183" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/analogs & derivatives/metabolism ; Allosteric Regulation ; Binding Sites ; Biotin/*metabolism ; Catalytic Domain ; Coenzyme A/metabolism ; Crystallography, X-Ray ; Dimerization ; Enzyme Activators/metabolism ; Models, Molecular ; Mutation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Pyruvate Carboxylase/*chemistry/genetics/*metabolism ; Rhizobium etli/*enzymology
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  • 31
    Publication Date: 2007-09-01
    Description: DNA replication in archaea and in eukaryotes share many similarities. We report the structure of an archaeal origin recognition complex protein, ORC1, bound to an origin recognition box, a DNA sequence that is found in multiple copies at replication origins. DNA binding is mediated principally by a C-terminal winged helix domain that inserts deeply into the major and minor grooves, widening them both. However, additional DNA contacts are made with the N-terminal AAA+ domain, which inserts into the minor groove at a characteristic G-rich sequence, inducing a 35 degrees bend in the duplex and providing directionality to the binding site. Both contact regions also induce substantial unwinding of the DNA. The structure provides insight into the initial step in assembly of a replication origin and recruitment of minichromosome maintenance (MCM) helicase to that origin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gaudier, Martin -- Schuwirth, Barbara S -- Westcott, Sarah L -- Wigley, Dale B -- New York, N.Y. -- Science. 2007 Aug 31;317(5842):1213-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research UK Clare Hall Laboratories, London Research Institute, Blanche Lane, South Mimms, Potters Bar, Herts EN6 3LD, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17761880" target="_blank"〉PubMed〈/a〉
    Keywords: Aeropyrum/*chemistry/metabolism ; Archaeal Proteins/*chemistry ; Binding Sites ; Crystallography, X-Ray ; DNA, Archaeal/*chemistry/metabolism ; Dimerization ; Models, Molecular ; Nucleic Acid Conformation ; Origin Recognition Complex/*chemistry ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; *Replication Origin
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  • 32
    Publication Date: 2007-02-03
    Description: Quantum mechanical analysis of electron tunneling in nine thermally fluctuating cytochrome b562 derivatives reveals two distinct protein-mediated coupling limits. A structure-insensitive regime arises for redox partners coupled through dynamically averaged multiple-coupling pathways (in seven of the nine derivatives) where heme-edge coupling leads to the multiple-pathway regime. A structure-dependent limit governs redox partners coupled through a dominant pathway (in two of the nine derivatives) where axial-ligand coupling generates the single-pathway limit and slower rates. This two-regime paradigm provides a unified description of electron transfer rates in 26 ruthenium-modified heme and blue-copper proteins, as well as in numerous photosynthetic proteins.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3523119/" 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/PMC3523119/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prytkova, Tatiana R -- Kurnikov, Igor V -- Beratan, David N -- R01 GM048043/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Feb 2;315(5812):622-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Chemistry and Biochemistry, Duke University, Durham, NC 27708, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17272715" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; Computer Simulation ; Cytochrome b Group/*chemistry/*metabolism ; Cytochromes c/chemistry ; *Electron Transport ; Histidine/chemistry ; Hydrogen Bonding ; Ligands ; Mathematics ; Models, Chemical ; Models, Molecular ; Oxidation-Reduction ; Physicochemical Phenomena ; Protein Conformation ; Protein Folding ; Ruthenium
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  • 33
    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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  • 34
    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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  • 35
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-09-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Georgescu, Roxana E -- O'Donnell, Mike -- GM38839/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Aug 31;317(5842):1181-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of DNA Replication, Howard Hughes Medical Institute, Rockefeller University, New York, NY 10065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17761872" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Aeropyrum/*chemistry/metabolism ; Archaeal Proteins/*chemistry/metabolism ; Binding Sites ; DNA, Archaeal/*chemistry/metabolism ; Dimerization ; Models, Molecular ; Nucleic Acid Conformation ; Origin Recognition Complex/*chemistry/*metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Replication Origin ; Sulfolobus solfataricus/*chemistry/metabolism
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  • 36
    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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  • 37
    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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  • 38
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    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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  • 39
    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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  • 40
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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〉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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  • 41
    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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  • 42
    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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  • 43
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    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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  • 44
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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〉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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 45
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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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  • 46
    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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  • 47
    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
    Print ISSN: 0036-8075
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  • 48
    Publication Date: 2007-06-16
    Description: Endotoxic lipopolysaccharide (LPS) with potent immunostimulatory activity is recognized by the receptor complex of MD-2 and Toll-like receptor 4. Crystal structures of human MD-2 and its complex with the antiendotoxic tetra-acylated lipid A core of LPS have been determined at 2.0 and 2.2 angstrom resolutions, respectively. MD-2 shows a deep hydrophobic cavity sandwiched by two beta sheets, in which four acyl chains of the ligand are fully confined. The phosphorylated glucosamine moieties are located at the entrance to the cavity. These structures suggest that MD-2 plays a principal role in endotoxin recognition and provide a basis for antiseptic drug development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ohto, Umeharu -- Fukase, Koichi -- Miyake, Kensuke -- Satow, Yoshinori -- New York, N.Y. -- Science. 2007 Jun 15;316(5831):1632-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17569869" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallography, X-Ray ; Fatty Acids/chemistry ; Glycolipids/*chemistry/metabolism ; Glycosylation ; Humans ; Hydrophobic and Hydrophilic Interactions ; Ligands ; Lipid A/*analogs & derivatives/chemistry/metabolism ; Lymphocyte Antigen 96/*chemistry/metabolism ; Models, Molecular ; Phosphorylation ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary
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  • 49
    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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  • 50
    Publication Date: 2007-08-11
    Description: Na+/H+ antiporters are central to cellular salt and pH homeostasis. The structure of Escherichia coli NhaA was recently determined, but its mechanisms of transport and pH regulation remain elusive. We performed molecular dynamics simulations of NhaA that, with existing experimental data, enabled us to propose an atomically detailed model of antiporter function. Three conserved aspartates are key to our proposed mechanism: Asp164 (D164) is the Na+-binding site, D163 controls the alternating accessibility of this binding site to the cytoplasm or periplasm, and D133 is crucial for pH regulation. Consistent with experimental stoichiometry, two protons are required to transport a single Na+ ion: D163 protonates to reveal the Na+-binding site to the periplasm, and subsequent protonation of D164 releases Na+. Additional mutagenesis experiments further validated the model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arkin, Isaiah T -- Xu, Huafeng -- Jensen, Morten O -- Arbely, Eyal -- Bennett, Estelle R -- Bowers, Kevin J -- Chow, Edmond -- Dror, Ron O -- Eastwood, Michael P -- Flitman-Tene, Ravenna -- Gregersen, Brent A -- Klepeis, John L -- Kolossvary, Istvan -- Shan, Yibing -- Shaw, David E -- New York, N.Y. -- Science. 2007 Aug 10;317(5839):799-803.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉D. E. Shaw Research, New York, NY 10036, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17690293" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid/metabolism ; Binding Sites ; Computer Simulation ; Crystallization ; Cytoplasm/metabolism ; Escherichia coli/growth & development/*metabolism ; Escherichia coli Proteins/*chemistry/*metabolism ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Ion Transport ; *Models, Biological ; Models, Molecular ; Mutagenesis ; Periplasm/metabolism ; Protein Conformation ; Protein Structure, Secondary ; *Protons ; Sodium/*metabolism ; Sodium-Hydrogen Antiporter/*chemistry/*metabolism
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  • 51
    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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  • 52
    Publication Date: 2007-11-10
    Description: DNA polymerase eta (Pol eta) is a eukaryotic lesion bypass polymerase that helps organisms to survive exposure to ultraviolet (UV) radiation, and tumor cells to gain resistance against cisplatin-based chemotherapy. It allows cells to replicate across cross-link lesions such as 1,2-d(GpG) cisplatin adducts (Pt-GG) and UV-induced cis-syn thymine dimers. We present structural and biochemical analysis of how Pol eta copies Pt-GG-containing DNA. The damaged DNA is bound in an open DNA binding rim. Nucleotidyl transfer requires the DNA to rotate into an active conformation, driven by hydrogen bonding of the templating base to the dNTP. For the 3'dG of the Pt-GG, this step is accomplished by a Watson-Crick base pair to dCTP and is biochemically efficient and accurate. In contrast, bypass of the 5'dG of the Pt-GG is less efficient and promiscuous for dCTP and dATP as a result of the presence of the rigid Pt cross-link. Our analysis reveals the set of structural features that enable Pol eta to replicate across strongly distorting DNA lesions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alt, Aaron -- Lammens, Katja -- Chiocchini, Claudia -- Lammens, Alfred -- Pieck, J Carsten -- Kuch, David -- Hopfner, Karl-Peter -- Carell, Thomas -- New York, N.Y. -- Science. 2007 Nov 9;318(5852):967-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Munich Center for Integrated Protein Science (CiPS), Ludwig Maximilians University, D-81377 Munich, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17991862" target="_blank"〉PubMed〈/a〉
    Keywords: Antineoplastic Agents/metabolism/*pharmacology ; Base Pairing ; Binding Sites ; Cisplatin/analogs & derivatives/chemistry/metabolism/*pharmacology ; Crystallization ; Crystallography, X-Ray ; DNA/chemistry/*metabolism ; DNA Adducts/chemistry/*metabolism ; *DNA Damage ; DNA Replication ; DNA-Directed DNA Polymerase/chemistry/genetics/*metabolism ; Deoxycytosine Nucleotides/chemistry/metabolism ; Hydrogen Bonding ; Models, Molecular ; Mutagenesis, Site-Directed ; Nucleic Acid Conformation ; Protein Conformation ; Protein Structure, Tertiary ; Templates, Genetic
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  • 53
    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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  • 54
    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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  • 55
    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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  • 56
    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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  • 57
    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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  • 58
    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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  • 59
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    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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  • 60
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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
    Print ISSN: 0036-8075
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  • 61
    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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  • 62
    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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    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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  • 64
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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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  • 65
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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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  • 66
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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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  • 67
    Publication Date: 2007-06-30
    Description: Leukotrienes are proinflammatory products of arachidonic acid oxidation by 5-lipoxygenase that have been shown to be involved in respiratory and cardiovascular diseases. The integral membrane protein FLAP is essential for leukotriene biosynthesis. We describe the x-ray crystal structures of human FLAP in complex with two leukotriene biosynthesis inhibitors at 4.0 and 4.2 angstrom resolution, respectively. The structures show that inhibitors bind in membrane-embedded pockets of FLAP, which suggests how these inhibitors prevent arachidonic acid from binding to FLAP and subsequently being transferred to 5-lipoxygenase, thereby preventing leukotriene biosynthesis. This structural information provides a platform for the development of therapeutics for respiratory and cardiovascular diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferguson, Andrew D -- McKeever, Brian M -- Xu, Shihua -- Wisniewski, Douglas -- Miller, Douglas K -- Yamin, Ting-Ting -- Spencer, Robert H -- Chu, Lin -- Ujjainwalla, Feroze -- Cunningham, Barry R -- Evans, Jilly F -- Becker, Joseph W -- New York, N.Y. -- Science. 2007 Jul 27;317(5837):510-2. Epub 2007 Jun 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicinal Chemistry, Merck Research Laboratories, Rahway, NJ 07065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17600184" target="_blank"〉PubMed〈/a〉
    Keywords: 5-Lipoxygenase-Activating Proteins ; Arachidonate 5-Lipoxygenase/metabolism ; Arachidonic Acid/metabolism ; Binding Sites ; Carrier Proteins/antagonists & inhibitors/*chemistry/genetics/metabolism ; Catalytic Domain ; Crystallography, X-Ray ; Cytosol/chemistry ; Humans ; Hydrophobic and Hydrophilic Interactions ; Indoles/*chemistry/metabolism/pharmacology ; Membrane Proteins/antagonists & inhibitors/*chemistry/genetics/metabolism ; Models, Molecular ; Mutagenesis ; Nuclear Envelope/chemistry ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Quinolines/*chemistry/metabolism/pharmacology
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  • 68
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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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  • 69
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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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  • 70
    Publication Date: 2007-10-20
    Description: The complex between the DnaB helicase and the DnaG primase unwinds duplex DNA at the eubacterial replication fork and synthesizes the Okazaki RNA primers. The crystal structures of hexameric DnaB and its complex with the helicase binding domain (HBD) of DnaG reveal that within the hexamer the two domains of DnaB pack with strikingly different symmetries to form a distinct two-layered ring structure. Each of three bound HBDs stabilizes the DnaB hexamer in a conformation that may increase its processivity. Three positive, conserved electrostatic patches on the N-terminal domain of DnaB may also serve as a binding site for DNA and thereby guide the DNA to a DnaG active site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bailey, Scott -- Eliason, William K -- Steitz, Thomas A -- GM57510/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Oct 19;318(5849):459-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry and Howard Hughes Medical Institute, Yale University, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17947583" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA Primase/*chemistry/metabolism ; DNA, Bacterial/chemistry/metabolism ; Dimerization ; DnaB Helicases/*chemistry/metabolism ; Endodeoxyribonucleases/chemistry/metabolism ; Escherichia coli/chemistry/enzymology/metabolism ; Escherichia coli Proteins/chemistry/metabolism ; Exodeoxyribonucleases/chemistry/metabolism ; Geobacillus stearothermophilus/*enzymology/metabolism ; Image Processing, Computer-Assisted ; Models, Molecular ; Protein Binding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary
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  • 71
    Publication Date: 2007-10-27
    Description: Heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors constitute the largest family of eukaryotic signal transduction proteins that communicate across the membrane. We report the crystal structure of a human beta2-adrenergic receptor-T4 lysozyme fusion protein bound to the partial inverse agonist carazolol at 2.4 angstrom resolution. The structure provides a high-resolution view of a human G protein-coupled receptor bound to a diffusible ligand. Ligand-binding site accessibility is enabled by the second extracellular loop, which is held out of the binding cavity by a pair of closely spaced disulfide bridges and a short helical segment within the loop. Cholesterol, a necessary component for crystallization, mediates an intriguing parallel association of receptor molecules in the crystal lattice. Although the location of carazolol in the beta2-adrenergic receptor is very similar to that of retinal in rhodopsin, structural differences in the ligand-binding site and other regions highlight the challenges in using rhodopsin as a template model for this large receptor family.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2583103/" 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/PMC2583103/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cherezov, Vadim -- Rosenbaum, Daniel M -- Hanson, Michael A -- Rasmussen, Soren G F -- Thian, Foon Sun -- Kobilka, Tong Sun -- Choi, Hee-Jung -- Kuhn, Peter -- Weis, William I -- Kobilka, Brian K -- Stevens, Raymond C -- F32 GM082028/GM/NIGMS NIH HHS/ -- GM075915/GM/NIGMS NIH HHS/ -- NS028471/NS/NINDS NIH HHS/ -- P50 GM062411/GM/NIGMS NIH HHS/ -- P50 GM073197/GM/NIGMS NIH HHS/ -- P50 GM073197-04/GM/NIGMS NIH HHS/ -- R01 GM056169/GM/NIGMS NIH HHS/ -- R01 GM089857/GM/NIGMS NIH HHS/ -- R21 GM075811/GM/NIGMS NIH HHS/ -- U54 GM074961/GM/NIGMS NIH HHS/ -- U54 GM074961-030001/GM/NIGMS NIH HHS/ -- Y1-CO-1020/CO/NCI NIH HHS/ -- Y1-GM-1104/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Nov 23;318(5854):1258-65. Epub 2007 Oct 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17962520" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage T4/enzymology ; Binding Sites ; Cell Membrane/chemistry/metabolism ; Cholesterol/chemistry/metabolism ; Crystallization ; Crystallography, X-Ray ; Drug Inverse Agonism ; Humans ; Ligands ; Models, Molecular ; Muramidase/chemistry/metabolism ; Propanolamines/chemistry/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Receptors, Adrenergic, beta-2/*chemistry/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Rhodopsin/chemistry/metabolism ; Static Electricity
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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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  • 73
    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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  • 74
    Publication Date: 2007-11-03
    Description: Quinoxalinedione compounds such as 6-cyano-7-nitroquinoxaline-2,3-dione (CNQX) are the most commonly used alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor antagonists. However, we find that in the presence of transmembrane AMPA receptor regulatory proteins (TARPs), which are AMPA receptor auxiliary subunits, CNQX acts as a partial agonist. CNQX induced small depolarizing currents in neurons of the central nervous system, and reconstitution of this agonist activity required coexpression of TARPs. A crystal structure of CNQX bound to the TARP-less AMPA receptor ligand-binding domain showed that, although CNQX induces partial domain closure, this movement is not transduced into linker separation, suggesting that TARPs may increase agonist efficacy by strengthening the coupling between domain closure and channel opening. Our results demonstrate that the presence of an auxiliary subunit can determine whether a compound functions as an agonist or antagonist.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Menuz, Karen -- Stroud, Robert M -- Nicoll, Roger A -- Hays, Franklin A -- GM078754/GM/NIGMS NIH HHS/ -- P50 GM73210/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Nov 2;318(5851):815-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California at San Francisco, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17975069" target="_blank"〉PubMed〈/a〉
    Keywords: 6-Cyano-7-nitroquinoxaline-2,3-dione/chemistry/*pharmacology ; Animals ; Benzodiazepines/pharmacology ; Binding, Competitive ; Cell Line ; Cerebellum/cytology ; Crystallography, X-Ray ; *Drug Partial Agonism ; Hippocampus/cytology ; Humans ; In Vitro Techniques ; Interneurons/drug effects ; Mice ; Models, Molecular ; Patch-Clamp Techniques ; Protein Conformation ; Protein Subunits/*physiology ; Pyramidal Cells/drug effects/metabolism ; Quinoxalines/pharmacology ; Receptors, AMPA/*agonists/*antagonists & inhibitors ; Structure-Activity Relationship ; Synaptic Transmission/drug effects ; Trichlormethiazide/pharmacology
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  • 75
    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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  • 76
    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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  • 77
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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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  • 78
    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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  • 79
    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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  • 80
    Publication Date: 2007-04-21
    Description: Iron-peroxide intermediates are central in the reaction cycle of many iron-containing biomolecules. We trapped iron(III)-(hydro)peroxo species in crystals of superoxide reductase (SOR), a nonheme mononuclear iron enzyme that scavenges superoxide radicals. X-ray diffraction data at 1.95 angstrom resolution and Raman spectra recorded in crystallo revealed iron-(hydro)peroxo intermediates with the (hydro)peroxo group bound end-on. The dynamic SOR active site promotes the formation of transient hydrogen bond networks, which presumably assist the cleavage of the iron-oxygen bond in order to release the reaction product, hydrogen peroxide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Katona, Gergely -- Carpentier, Philippe -- Niviere, Vincent -- Amara, Patricia -- Adam, Virgile -- Ohana, Jeremy -- Tsanov, Nikolay -- Bourgeois, Dominique -- New York, N.Y. -- Science. 2007 Apr 20;316(5823):449-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Biologie Structurale (IBS) Jean-Pierre Ebel, Commissariat a l'Energie Atomique (CEA), Centre National de la Recherche Scientifique (CNRS), Universite Joseph Fourier, 41 rue Jules Horowitz, F-38027 Grenoble, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17446401" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallization ; Crystallography, X-Ray ; Deltaproteobacteria/*enzymology ; Ferric Compounds/chemistry/metabolism ; Hydrogen Bonding ; Hydrogen Peroxide/*chemistry/metabolism ; Iron/*chemistry ; Ligands ; Models, Chemical ; Models, Molecular ; Oxidation-Reduction ; Oxidoreductases/*chemistry/*metabolism ; Oxygen/chemistry ; Peroxides/*chemistry ; Protein Conformation ; Protons ; Spectrum Analysis, Raman
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  • 81
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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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  • 82
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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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  • 83
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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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  • 84
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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
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  • 85
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-03-03
    Description: Theory suggests that the current rapid increase in connectivity and consequential changes in the structure of human, agricultural, and wildlife populations may select for parasite strains with higher infectivity. We carried out a test of this spatial theory by experimentally altering individual host movement rates in a model host/pathogen system by altering the viscosity of their environment. In our microevolutionary selection experiments, the infectivity of the virus was, as predicted by the theory, reduced in the most viscous populations. We therefore provide empirical support for the theory that population structure affects the evolution of infectious organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boots, Michael -- Mealor, Michael -- New York, N.Y. -- Science. 2007 Mar 2;315(5816):1284-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Animal and Plant Sciences, University of Sheffield, Western Bank, Sheffield S10 2TN, UK. m.boots@sheffield.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17332415" target="_blank"〉PubMed〈/a〉
    Keywords: Analysis of Variance ; Animals ; *Biological Evolution ; Food ; Granulovirus/*pathogenicity/physiology ; Larva/physiology/virology ; Moths/physiology/*virology ; Movement ; Selection, Genetic ; Viscosity
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  • 86
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-03-03
    Description: Halkieriids and wiwaxiids are cosmopolitan sclerite-bearing metazoans from the Lower and Middle Cambrian. Although they have similar scleritomes, their phylogenetic position is contested. A new scleritomous fossil from the Burgess Shale has the prominent anterior shell of the halkieriids but also bears wiwaxiid-like sclerites. This new fossil defines the monophyletic halwaxiids and indicates that they have a key place in early lophotrochozoan history.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morris, Simon Conway -- Caron, Jean-Bernard -- New York, N.Y. -- Science. 2007 Mar 2;315(5816):1255-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth Sciences, University of Cambridge, Cambridge CB2 3EQ, UK. sc113@esc.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17332408" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Annelida/anatomy & histology/classification ; *Biological Evolution ; *Fossils ; Invertebrates/anatomy & histology/*classification ; Mollusca/anatomy & histology/classification ; Phylogeny
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  • 87
    Publication Date: 2007-09-29
    Description: The genome of the eukaryotic protist Giardia lamblia, an important human intestinal parasite, is compact in structure and content, contains few introns or mitochondrial relics, and has simplified machinery for DNA replication, transcription, RNA processing, and most metabolic pathways. Protein kinases comprise the single largest protein class and reflect Giardia's requirement for a complex signal transduction network for coordinating differentiation. Lateral gene transfer from bacterial and archaeal donors has shaped Giardia's genome, and previously unknown gene families, for example, cysteine-rich structural proteins, have been discovered. Unexpectedly, the genome shows little evidence of heterozygosity, supporting recent speculations that this organism is sexual. This genome sequence will not only be valuable for investigating the evolution of eukaryotes, but will also be applied to the search for new therapeutics for this parasite.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morrison, Hilary G -- McArthur, Andrew G -- Gillin, Frances D -- Aley, Stephen B -- Adam, Rodney D -- Olsen, Gary J -- Best, Aaron A -- Cande, W Zacheus -- Chen, Feng -- Cipriano, Michael J -- Davids, Barbara J -- Dawson, Scott C -- Elmendorf, Heidi G -- Hehl, Adrian B -- Holder, Michael E -- Huse, Susan M -- Kim, Ulandt U -- Lasek-Nesselquist, Erica -- Manning, Gerard -- Nigam, Anuranjini -- Nixon, Julie E J -- Palm, Daniel -- Passamaneck, Nora E -- Prabhu, Anjali -- Reich, Claudia I -- Reiner, David S -- Samuelson, John -- Svard, Staffan G -- Sogin, Mitchell L -- AI42488/AI/NIAID NIH HHS/ -- AI43273/AI/NIAID NIH HHS/ -- AI51687/AI/NIAID NIH HHS/ -- R01 AI043273/AI/NIAID NIH HHS/ -- R01 AI048082/AI/NIAID NIH HHS/ -- R01 HG004164/HG/NHGRI NIH HHS/ -- R01 HG004164-01/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2007 Sep 28;317(5846):1921-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Marine Biological Laboratory, Woods Hole, MA 02543-1015, USA. morrison@mbl.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17901334" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Biological Evolution ; DNA Replication/genetics ; *Eukaryotic Cells ; Gene Transfer, Horizontal ; Genes, Protozoan ; *Genome, Protozoan ; Genomics ; Giardia lamblia/classification/*genetics/physiology ; Metabolic Networks and Pathways/genetics ; Molecular Sequence Data ; Phylogeny ; Protein Kinases/genetics/metabolism ; Protozoan Proteins/chemistry/genetics/metabolism ; RNA Processing, Post-Transcriptional ; Signal Transduction ; Transcription, Genetic
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  • 88
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-03-17
    Description: Life originated, according to the RNA World hypothesis, from self-replicating ribozymes that catalyzed ligation of RNA fragments. We have solved the 2.6 angstrom crystal structure of a ligase ribozyme that catalyzes regiospecific formation of a 5' to 3' phosphodiester bond between the 5'-triphosphate and the 3'-hydroxyl termini of two RNA fragments. Invariant residues form tertiary contacts that stabilize a flexible stem of the ribozyme at the ligation site, where an essential magnesium ion coordinates three phosphates. The structure of the active site permits us to suggest how transition-state stabilization and a general base may catalyze the ligation reaction required for prebiotic RNA assembly.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Robertson, Michael P -- Scott, William G -- New York, N.Y. -- Science. 2007 Mar 16;315(5818):1549-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for the Molecular Biology of RNA and Department of Chemistry and Biochemistry, Robert L. Sinsheimer Laboratories, University of California, Santa Cruz, Santa Cruz, CA 95064, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17363667" target="_blank"〉PubMed〈/a〉
    Keywords: Base Pairing ; Binding Sites ; Catalysis ; Catalytic Domain ; Crystallization ; Crystallography, X-Ray ; Directed Molecular Evolution ; Hydrogen Bonding ; Models, Molecular ; Molecular Conformation ; Nucleic Acid Conformation ; Oligoribonucleotides/chemistry/metabolism ; RNA, Catalytic/*chemistry/metabolism ; Ribonucleotides/chemistry/metabolism ; Templates, Genetic
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  • 89
    Publication Date: 2007-02-10
    Description: Glycoprotein G of the vesicular stomatitis virus triggers membrane fusion via a low pH-induced structural rearrangement. Despite the equilibrium between the pre- and postfusion states, the structure of the prefusion form, determined to 3.0 angstrom resolution, shows that the fusogenic transition entails an extensive structural reorganization of G. Comparison with the structure of the postfusion form suggests a pathway for the conformational change. In the prefusion form, G has the shape of a tripod with the fusion loops exposed, which point toward the viral membrane, and with the antigenic sites located at the distal end of the molecule. A large number of G glycoproteins, perhaps organized as in the crystals, act cooperatively to induce membrane merging.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roche, Stephane -- Rey, Felix A -- Gaudin, Yves -- Bressanelli, Stephane -- New York, N.Y. -- Science. 2007 Feb 9;315(5813):843-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CNRS, Unite Mixte de Recherche (UMR) 2472, Institut National de la Recherche Agronomique (INRA), UMR 1157, Institut Federatif de Recherche 115, Laboratoire de Virologie Moleculaire et Structurale, 91198, Gif sur Yvette, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17289996" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Crystallization ; Crystallography, X-Ray ; Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; Membrane Fusion ; Membrane Glycoproteins/*chemistry ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Vesicular stomatitis Indiana virus/*chemistry ; Viral Envelope Proteins/*chemistry ; Viral Fusion Proteins/*chemistry
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  • 90
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-12-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kerr, Richard A -- New York, N.Y. -- Science. 2007 Dec 21;318(5858):1854.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18096781" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; *Biological Evolution ; *Fossils ; Geologic Sediments/chemistry ; *Invertebrates/classification ; *Minor Planets
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  • 91
    Publication Date: 2007-07-28
    Description: NS3, an essential helicase for replication of hepatitis C virus, is a model enzyme for investigating helicase function. Using single-molecule fluorescence analysis, we showed that NS3 unwinds DNA in discrete steps of about three base pairs (bp). Dwell time analysis indicated that about three hidden steps are required before a 3-bp step is taken. Taking into account the available structural data, we propose a spring-loaded mechanism in which several steps of one nucleotide per adenosine triphosphate molecule accumulate tension on the protein-DNA complex, which is relieved periodically via a burst of 3-bp unwinding. NS3 appears to shelter the displaced strand during unwinding, and, upon encountering a barrier or after unwinding 〉18 bp, it snaps or slips backward rapidly and repeats unwinding many times in succession. Such repetitive unwinding behavior over a short stretch of duplex may help to keep secondary structures resolved during viral genome replication.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3565428/" 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/PMC3565428/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Myong, Sua -- Bruno, Michael M -- Pyle, Anna M -- Ha, Taekjip -- R01 GM060620/GM/NIGMS NIH HHS/ -- R01 GM065367/GM/NIGMS NIH HHS/ -- R01-GM060620/GM/NIGMS NIH HHS/ -- R01-GM065367/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2007 Jul 27;317(5837):513-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Physics Department, University of Illinois, 1110 West Green Street, Urbana, IL 61801, USA. smyong@uiuc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17656723" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Base Pairing ; DNA/chemistry/*metabolism ; DNA Helicases/*metabolism ; Fluorescence Resonance Energy Transfer ; Hepacivirus/*enzymology ; Models, Biological ; Models, Molecular ; Nucleic Acid Conformation ; Temperature ; Viral Nonstructural Proteins/chemistry/*metabolism
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  • 92
    Publication Date: 2007-11-10
    Description: An unexpected biochemical strategy for chain initiation is described for the loading module of the polyketide synthase of curacin A, an anticancer lead derived from the marine cyanobacterium Lyngbya majuscula. A central GCN5-related N-acetyltransferase (GNAT) domain bears bifunctional decarboxylase/S-acetyltransferase activity, both unprecedented for the GNAT superfamily. A CurA loading tridomain, consisting of an adaptor domain, the GNAT domain, and an acyl carrier protein, was assessed biochemically, revealing that a domain showing homology to GNAT (GNAT(L)) catalyzes (i) decarboxylation of malonyl-coenzyme A (malonyl-CoA) to acetyl-CoA and (ii) direct S-acetyl transfer from acetyl-CoA to load an adjacent acyl carrier protein domain (ACP(L)). Moreover, the N-terminal adapter domain was shown to facilitate acetyl-group transfer. Crystal structures of GNAT(L) were solved at 1.95 angstroms (ligand-free form) and 2.75 angstroms (acyl-CoA complex), showing distinct substrate tunnels for acyl-CoA and holo-ACP(L) binding. Modeling and site-directed mutagenesis experiments demonstrated that histidine-389 and threonine-355, at the convergence of the CoA and ACP tunnels, participate in malonyl-CoA decarboxylation but not in acetyl-group transfer. Decarboxylation precedes acetyl-group transfer, leading to acetyl-ACP(L) as the key curacin A starter unit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gu, Liangcai -- Geders, Todd W -- Wang, Bo -- Gerwick, William H -- Hakansson, Kristina -- Smith, Janet L -- Sherman, David H -- DK42303/DK/NIDDK NIH HHS/ -- GM076477/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Nov 9;318(5852):970-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17991863" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyl Coenzyme A/metabolism ; Acetyltransferases/*chemistry/*metabolism ; Acyl Carrier Protein/chemistry/metabolism ; Amino Acid Sequence ; Carboxy-Lyases/chemistry/metabolism ; Crystallography, X-Ray ; Cyanobacteria/*enzymology/genetics ; Cyclopropanes/*metabolism ; Decarboxylation ; Malonyl Coenzyme A/metabolism ; Models, Molecular ; Molecular Sequence Data ; Polyketide Synthases/*chemistry/genetics/*metabolism ; Protein Conformation ; Protein Structure, Tertiary ; Thiazoles/*metabolism
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  • 93
    Publication Date: 2007-10-20
    Description: Nonhomologous end joining (NHEJ) is a critical DNA double-strand break (DSB) repair pathway required to maintain genome stability. Many prokaryotes possess a minimalist NHEJ apparatus required to repair DSBs during stationary phase, composed of two conserved core proteins, Ku and ligase D (LigD). The crystal structure of Mycobacterium tuberculosis polymerase domain of LigD mediating the synapsis of two noncomplementary DNA ends revealed a variety of interactions, including microhomology base pairing, mismatched and flipped-out bases, and 3' termini forming hairpin-like ends. Biochemical and biophysical studies confirmed that polymerase-induced end synapsis also occurs in solution. We propose that this DNA synaptic structure reflects an intermediate bridging stage of the NHEJ process, before end processing and ligation, with both the polymerase and the DNA sequence playing pivotal roles in determining the sequential order of synapsis and remodeling before end joining.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brissett, Nigel C -- Pitcher, Robert S -- Juarez, Raquel -- Picher, Angel J -- Green, Andrew J -- Dafforn, Timothy R -- Fox, Gavin C -- Blanco, Luis -- Doherty, Aidan J -- BB/D522746/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- G120/738/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2007 Oct 19;318(5849):456-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genome Damage and Stability Centre, University of Sussex, Brighton BN1 9RQ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17947582" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Crystallography, X-Ray ; DNA Ligases/*chemistry/genetics/metabolism ; *DNA Repair ; DNA, Bacterial/*chemistry/metabolism ; Dimerization ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Mycobacterium tuberculosis/*chemistry/enzymology/genetics/metabolism ; Protein Conformation ; Protein Structure, Tertiary
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  • 94
    Publication Date: 2007-10-27
    Description: The beta2-adrenergic receptor (beta2AR) is a well-studied prototype for heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors (GPCRs) that respond to diffusible hormones and neurotransmitters. To overcome the structural flexibility of the beta2AR and to facilitate its crystallization, we engineered a beta2AR fusion protein in which T4 lysozyme (T4L) replaces most of the third intracellular loop of the GPCR ("beta2AR-T4L") and showed that this protein retains near-native pharmacologic properties. Analysis of adrenergic receptor ligand-binding mutants within the context of the reported high-resolution structure of beta2AR-T4L provides insights into inverse-agonist binding and the structural changes required to accommodate catecholamine agonists. Amino acids known to regulate receptor function are linked through packing interactions and a network of hydrogen bonds, suggesting a conformational pathway from the ligand-binding pocket to regions that interact with G proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosenbaum, Daniel M -- Cherezov, Vadim -- Hanson, Michael A -- Rasmussen, Soren G F -- Thian, Foon Sun -- Kobilka, Tong Sun -- Choi, Hee-Jung -- Yao, Xiao-Jie -- Weis, William I -- Stevens, Raymond C -- Kobilka, Brian K -- F32 GM082028/GM/NIGMS NIH HHS/ -- NS028471/NS/NINDS NIH HHS/ -- P50 GM073197/GM/NIGMS NIH HHS/ -- P50 GM62411/GM/NIGMS NIH HHS/ -- R01 GM056169/GM/NIGMS NIH HHS/ -- R21 GM075811/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Nov 23;318(5854):1266-73. Epub 2007 Oct 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17962519" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenergic beta-Agonists/chemistry/metabolism ; Adrenergic beta-Antagonists/chemistry/metabolism ; Amino Acid Sequence ; Bacteriophage T4/enzymology ; Binding Sites ; Cell Line ; Cell Membrane/chemistry/metabolism ; Crystallization ; Crystallography, X-Ray ; Drug Inverse Agonism ; Humans ; Immunoglobulin Fab Fragments/chemistry/metabolism ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Muramidase/chemistry/metabolism ; Propanolamines/chemistry/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Receptors, Adrenergic, beta-2/*chemistry/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism
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  • 95
    Publication Date: 2007-04-07
    Description: Although highly homologous, the spliceosomal hPrp31 and the nucleolar Nop56 and Nop58 (Nop56/58) proteins recognize different ribonucleoprotein (RNP) particles. hPrp31 interacts with complexes containing the 15.5K protein and U4 or U4atac small nuclear RNA (snRNA), whereas Nop56/58 associate with 15.5K-box C/D small nucleolar RNA complexes. We present structural and biochemical analyses of hPrp31-15.5K-U4 snRNA complexes that show how the conserved Nop domain in hPrp31 maintains high RNP binding selectivity despite relaxed RNA sequence requirements. The Nop domain is a genuine RNP binding module, exhibiting RNA and protein binding surfaces. Yeast two-hybrid analyses suggest a link between retinitis pigmentosa and an aberrant hPrp31-hPrp6 interaction that blocks U4/U6-U5 tri-snRNP formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Sunbin -- Li, Ping -- Dybkov, Olexandr -- Nottrott, Stephanie -- Hartmuth, Klaus -- Luhrmann, Reinhard -- Carlomagno, Teresa -- Wahl, Markus C -- New York, N.Y. -- Science. 2007 Apr 6;316(5821):115-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Abteilung Zellulare Biochemie, Max-Planck-Institut fur Biophysikalische Chemie, Am Fassberg 11, D-37077 Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17412961" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Amino Acid Substitution ; Carrier Proteins/chemistry/metabolism ; Eye Proteins/*chemistry/*metabolism ; Humans ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA, Small Nuclear/*chemistry/*metabolism ; RNA-Binding Proteins ; Retinitis Pigmentosa/genetics ; Ribonucleoprotein, U4-U6 Small Nuclear/*chemistry/*metabolism ; Transcription Factors
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  • 96
    Publication Date: 2007-12-22
    Description: The guanine nucleotide exchange factor p63RhoGEF is an effector of the heterotrimeric guanine nucleotide-binding protein (G protein) Galphaq and thereby links Galphaq-coupled receptors (GPCRs) to the activation of the small-molecular-weight G protein RhoA. We determined the crystal structure of the Galphaq-p63RhoGEF-RhoA complex, detailing the interactions of Galphaq with the Dbl and pleckstrin homology (DH and PH) domains of p63RhoGEF. These interactions involve the effector-binding site and the C-terminal region of Galphaq and appear to relieve autoinhibition of the catalytic DH domain by the PH domain. Trio, Duet, and p63RhoGEF are shown to constitute a family of Galphaq effectors that appear to activate RhoA both in vitro and in intact cells. We propose that this structure represents the crux of an ancient signal transduction pathway that is expected to be important in an array of physiological processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lutz, Susanne -- Shankaranarayanan, Aruna -- Coco, Cassandra -- Ridilla, Marc -- Nance, Mark R -- Vettel, Christiane -- Baltus, Doris -- Evelyn, Chris R -- Neubig, Richard R -- Wieland, Thomas -- Tesmer, John J G -- HL071818/HL/NHLBI NIH HHS/ -- HL086865/HL/NHLBI NIH HHS/ -- Y1-CO-1020/CO/NCI NIH HHS/ -- Y1-GM-1104/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Dec 21;318(5858):1923-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Experimental and Clinical Pharmacology and Toxicology, Medical Faculty Mannheim, University of Heidelberg, Maybachstrasse 14, D-68169 Mannheim, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18096806" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Cell Line ; Crystallography, X-Ray ; GTP-Binding Protein alpha Subunits, Gq-G11/*chemistry/metabolism ; Guanine Nucleotide Exchange Factors/*chemistry/metabolism ; Humans ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Rho Guanine Nucleotide Exchange Factors ; Signal Transduction ; rhoA GTP-Binding Protein/*chemistry/metabolism
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  • 97
    Publication Date: 2007-10-06
    Description: Interbreeding between species (hybridization) typically produces unfit offspring. Reduced hybridization should therefore be favored by natural selection. However, this is difficult to accomplish because hybridization also sets the stage for genetic recombination to dissociate species-specific traits from the preferences for them. Here we show that this association is maintained by physical linkage (on the same chromosome) in two hybridizing Ficedula flycatchers. By analyzing the mating patterns of female hybrids and cross-fostered offspring, we demonstrate that species recognition is inherited on the Z chromosome, which is also the known location of species-specific male plumage traits and genes causing low hybrid fitness. Limited recombination on the Z chromosome maintains associations of Z-linked genes despite hybridization, suggesting that the sex chromosomes may be a hotspot for adaptive speciation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saether, Stein A -- Saetre, Glenn-Peter -- Borge, Thomas -- Wiley, Chris -- Svedin, Nina -- Andersson, Gunilla -- Veen, Thor -- Haavie, Jon -- Servedio, Maria R -- Bures, Stanislav -- Kral, Miroslav -- Hjernquist, Marten B -- Gustafsson, Lars -- Traff, Johan -- Qvarnstrom, Anna -- New York, N.Y. -- Science. 2007 Oct 5;318(5847):95-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Animal Population Biology, Netherlands Institute of Ecology, Post Office Box 40, 6666 ZG Heteren, Netherlands. s.a.sather@bio.uio.no〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17916732" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Feathers ; Female ; Gene Flow ; *Genetic Linkage ; *Genetic Speciation ; Hybridization, Genetic ; Male ; *Mating Preference, Animal ; Recombination, Genetic ; Reproduction ; Sex Chromosomes/*genetics ; Sexual Behavior, Animal ; Songbirds/anatomy & histology/genetics/*physiology
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  • 98
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-03-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hardie, D Grahame -- New York, N.Y. -- Science. 2007 Mar 23;315(5819):1671-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Physiology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK. d.g.hardie@dundee.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17379794" target="_blank"〉PubMed〈/a〉
    Keywords: AMP-Activated Protein Kinases ; Adenosine Monophosphate/metabolism ; Adenosine Triphosphate/metabolism ; Catalytic Domain ; Crystallization ; Crystallography, X-Ray ; Humans ; Models, Molecular ; Multienzyme Complexes/*chemistry/*metabolism ; Phosphorylation ; Protein Kinases/chemistry ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism ; Protein-Serine-Threonine Kinases/*chemistry/*metabolism ; Schizosaccharomyces/*enzymology
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  • 99
    Publication Date: 2007-07-28
    Description: Unlike most of its close relatives, Arabidopsis thaliana is capable of self-pollination. In other members of the mustard family, outcrossing is ensured by the complex self-incompatibility (S) locus,which harbors multiple diverged specificity haplotypes that effectively prevent selfing. We investigated the role of the S locus in the evolution of and transition to selfing in A. thaliana. We found that the S locus of A. thaliana harbored considerable diversity, which is an apparent remnant of polymorphism in the outcrossing ancestor. Thus, the fixation of a single inactivated S-locus allele cannot have been a key step in the transition to selfing. An analysis of the genome-wide pattern of linkage disequilibrium suggests that selfing most likely evolved roughly a million years ago or more.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tang, Chunlao -- Toomajian, Christopher -- Sherman-Broyles, Susan -- Plagnol, Vincent -- Guo, Ya-Long -- Hu, Tina T -- Clark, Richard M -- Nasrallah, June B -- Weigel, Detlef -- Nordborg, Magnus -- GM62932/GM/NIGMS NIH HHS/ -- P50 HG002790/HG/NHGRI NIH HHS/ -- R01 GM062932/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Aug 24;317(5841):1070-2. Epub 2007 Jul 26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular and Computational Biology, University of Southern California, Los Angeles, CA 90089, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17656687" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Arabidopsis/*genetics/*physiology ; Arabidopsis Proteins/*genetics ; *Biological Evolution ; Chromosomes, Artificial, Bacterial ; *Genes, Plant ; Genetic Drift ; Haplotypes ; Linkage Disequilibrium ; Molecular Sequence Data ; Nuclear Proteins/*genetics ; Plant Proteins/*genetics ; Polymerase Chain Reaction ; Polymorphism, Genetic ; Protein Kinases/*genetics ; *Pseudogenes ; Reproduction/physiology
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  • 100
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-10-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arrow, Holly -- New York, N.Y. -- Science. 2007 Oct 26;318(5850):581-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychology, and the Institute of Cognitive and Decision Sciences, University of Oregon, Eugene, OR 97403-1227, USA. harrow@uoregon.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17962546" target="_blank"〉PubMed〈/a〉
    Keywords: *Altruism ; *Biological Evolution ; Computer Simulation ; Cooperative Behavior ; *Hostility ; Humans ; Models, Psychological ; *Social Behavior ; Warfare
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