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  • Articles  (14)
  • Molecular Sequence Data  (14)
  • 2000-2004  (14)
  • 2004  (14)
  • Medicine  (14)
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  • Articles  (14)
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  • 2000-2004  (14)
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  • 1
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    A draft sequence for the genome of the domesticated silkworm (Bombyx mori) (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-14
    Description: We report a draft sequence for the genome of the domesticated silkworm (Bombyx mori), covering 90.9% of all known silkworm genes. Our estimated gene count is 18,510, which exceeds the 13,379 genes reported for Drosophila melanogaster. Comparative analyses to fruitfly, mosquito, spider, and butterfly reveal both similarities and differences in gene content.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xia, Qingyou -- Zhou, Zeyang -- Lu, Cheng -- Cheng, Daojun -- Dai, Fangyin -- Li, Bin -- Zhao, Ping -- Zha, Xingfu -- Cheng, Tingcai -- Chai, Chunli -- Pan, Guoqing -- Xu, Jinshan -- Liu, Chun -- Lin, Ying -- Qian, Jifeng -- Hou, Yong -- Wu, Zhengli -- Li, Guanrong -- Pan, Minhui -- Li, Chunfeng -- Shen, Yihong -- Lan, Xiqian -- Yuan, Lianwei -- Li, Tian -- Xu, Hanfu -- Yang, Guangwei -- Wan, Yongji -- Zhu, Yong -- Yu, Maode -- Shen, Weide -- Wu, Dayang -- Xiang, Zhonghuai -- Yu, Jun -- Wang, Jun -- Li, Ruiqiang -- Shi, Jianping -- Li, Heng -- Li, Guangyuan -- Su, Jianning -- Wang, Xiaoling -- Li, Guoqing -- Zhang, Zengjin -- Wu, Qingfa -- Li, Jun -- Zhang, Qingpeng -- Wei, Ning -- Xu, Jianzhe -- Sun, Haibo -- Dong, Le -- Liu, Dongyuan -- Zhao, Shengli -- Zhao, Xiaolan -- Meng, Qingshun -- Lan, Fengdi -- Huang, Xiangang -- Li, Yuanzhe -- Fang, Lin -- Li, Changfeng -- Li, Dawei -- Sun, Yongqiao -- Zhang, Zhenpeng -- Yang, Zheng -- Huang, Yanqing -- Xi, Yan -- Qi, Qiuhui -- He, Dandan -- Huang, Haiyan -- Zhang, Xiaowei -- Wang, Zhiqiang -- Li, Wenjie -- Cao, Yuzhu -- Yu, Yingpu -- Yu, Hong -- Li, Jinhong -- Ye, Jiehua -- Chen, Huan -- Zhou, Yan -- Liu, Bin -- Wang, Jing -- Ye, Jia -- Ji, Hai -- Li, Shengting -- Ni, Peixiang -- Zhang, Jianguo -- Zhang, Yong -- Zheng, Hongkun -- Mao, Bingyu -- Wang, Wen -- Ye, Chen -- Li, Songgang -- Wang, Jian -- Wong, Gane Ka-Shu -- Yang, Huanming -- Biology Analysis Group -- 1 P50 HG02351/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2004 Dec 10;306(5703):1937-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Southwest Agricultural University, Chongqing Beibei, 400716, China. xiaqy@swau.cq.cn〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15591204" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Animals ; Anopheles/genetics ; Body Patterning/genetics ; Bombyx/*genetics/growth & development/metabolism ; Butterflies/genetics ; Computational Biology ; DNA Transposable Elements ; Drosophila melanogaster/genetics ; Exocrine Glands/metabolism ; Expressed Sequence Tags ; Female ; Genes, Homeobox ; *Genes, Insect ; *Genome ; Immunity, Innate/genetics ; Insect Hormones/genetics ; Insect Proteins/genetics ; Male ; Molecular Sequence Data ; *Sequence Analysis, DNA ; Sequence Homology, Nucleic Acid ; Sex Determination Processes ; Spiders/genetics ; Wings, Animal/growth & development
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Zebrafish Dpr2 inhibits mesoderm induction by promoting degradation of nodal receptors (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-02
    Description: Nodal proteins, members of the transforming growth factor-beta (TGFbeta) superfamily, have been identified as key endogenous mesoderm inducers in vertebrates. Precise control of Nodal signaling is essential for normal development of embryos. Here, we report that zebrafish dapper2 (dpr2) is expressed in mesoderm precursors during early embryogenesis and is positively regulated by Nodal signals. In vivo functional studies in zebrafish suggest that Dpr2 suppresses mesoderm induction activities of Nodal signaling. Dpr2 is localized in late endosomes, binds to the TGFbeta receptors ALK5 and ALK4, and accelerates lysosomal degradation of these receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Lixia -- Zhou, Hu -- Su, Ying -- Sun, Zhihui -- Zhang, Haiwen -- Zhang, Long -- Zhang, Yu -- Ning, Yuanheng -- Chen, Ye-Guang -- Meng, Anming -- New York, N.Y. -- Science. 2004 Oct 1;306(5693):114-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Developmental Biology, Ministry of Education (MOE), Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15459392" target="_blank"〉PubMed〈/a〉
    Keywords: Activin Receptors, Type I/*metabolism ; Amino Acid Sequence ; Animals ; Cell Line ; Embryo, Nonmammalian/embryology/*metabolism ; *Embryonic Induction ; Endosomes/metabolism ; Fluorescent Antibody Technique ; Gene Expression Profiling ; Gene Expression Regulation, Developmental ; Humans ; In Situ Hybridization ; Intracellular Signaling Peptides and Proteins ; Lysosomes/metabolism ; Mesoderm/*physiology ; Molecular Sequence Data ; Mutation ; Nodal Signaling Ligands ; Oligonucleotides, Antisense ; Protein-Serine-Threonine Kinases ; Proteins/metabolism ; Receptors, Transforming Growth Factor beta/*metabolism ; Signal Transduction ; Transforming Growth Factor beta/genetics/metabolism ; Zebrafish/*embryology/genetics/metabolism ; Zebrafish Proteins/chemistry/genetics/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Human PAD4 regulates histone arginine methylation levels via demethylimination (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-09-04
    Description: Methylation of arginine (Arg) and lysine residues in histones has been correlated with epigenetic forms of gene regulation. Although histone methyltransferases are known, enzymes that demethylate histones have not been identified. Here, we demonstrate that human peptidylarginine deiminase 4 (PAD4) regulates histone Arg methylation by converting methyl-Arg to citrulline and releasing methylamine. PAD4 targets multiple sites in histones H3 and H4, including those sites methylated by coactivators CARM1 (H3 Arg17) and PRMT1 (H4 Arg3). A decrease of histone Arg methylation, with a concomitant increase of citrullination, requires PAD4 activity in human HL-60 granulocytes. Moreover, PAD4 activity is linked with the transcriptional regulation of estrogen-responsive genes in MCF-7 cells. These data suggest that PAD4 mediates gene expression by regulating Arg methylation and citrullination in histones.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Yanming -- Wysocka, Joanna -- Sayegh, Joyce -- Lee, Young-Ho -- Perlin, Julie R -- Leonelli, Lauriebeth -- Sonbuchner, Lakshmi S -- McDonald, Charles H -- Cook, Richard G -- Dou, Yali -- Roeder, Robert G -- Clarke, Steven -- Stallcup, Michael R -- Allis, C David -- Coonrod, Scott A -- DK55274/DK/NIDDK NIH HHS/ -- GM R01 26020/GM/NIGMS NIH HHS/ -- GM R01 50659/GM/NIGMS NIH HHS/ -- HD R01 38353/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2004 Oct 8;306(5694):279-83. Epub 2004 Sep 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetic Medicine, Weill Medical College of Cornell University, 1300 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15345777" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arginine/*metabolism ; Blotting, Western ; Calcimycin/pharmacology ; Cell Line, Tumor ; Citrulline/metabolism ; Gene Expression Regulation ; Genes, Reporter ; HL-60 Cells ; Histones/*metabolism ; Humans ; Hydrolases/*metabolism ; Ionophores/pharmacology ; Membrane Proteins/genetics ; Methylamines/metabolism ; Methylation ; Molecular Sequence Data ; Presenilin-2 ; Promoter Regions, Genetic ; Protein-Arginine N-Methyltransferases/metabolism ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Use of CD134 as a primary receptor by the feline immunodeficiency virus (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-02-21
    Description: Feline immunodeficiency virus (FIV) induces a disease similar to acquired immunodeficiency syndrome (AIDS) in cats, yet in contrast to human immunodeficiency virus (HIV), CD4 is not the viral receptor. We identified a primary receptor for FIV as CD134 (OX40), a T cell activation antigen and costimulatory molecule. CD134 expression promotes viral binding and renders cells permissive for viral entry, productive infection, and syncytium formation. Infection is CXCR4-dependent, analogous to infection with X4 strains of HIV. Thus, despite the evolutionary divergence of the feline and human lentiviruses, both viruses use receptors that target the virus to a subset of cells that are pivotal to the acquired immune response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shimojima, Masayuki -- Miyazawa, Takayuki -- Ikeda, Yasuhiro -- McMonagle, Elizabeth L -- Haining, Hayley -- Akashi, Hiroomi -- Takeuchi, Yasuhiro -- Hosie, Margaret J -- Willett, Brian J -- R01 AI49765-01A1/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 20;303(5661):1192-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Veterinary Microbiology, Graduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14976315" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; CD4-Positive T-Lymphocytes/immunology/metabolism/virology ; Cats ; Cell Line ; Cell Line, Tumor ; DNA, Complementary ; Gene Library ; HIV/metabolism ; HeLa Cells ; Heterocyclic Compounds/pharmacology ; Humans ; Immunodeficiency Virus, Feline/*metabolism/pathogenicity ; Mice ; Molecular Sequence Data ; NIH 3T3 Cells ; Receptors, CXCR4/antagonists & inhibitors/metabolism ; Receptors, OX40 ; Receptors, Tumor Necrosis Factor/chemistry/genetics/immunology/*metabolism ; Receptors, Virus/chemistry/genetics/immunology/*metabolism ; Species Specificity ; Transduction, Genetic ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Environmental genome shotgun sequencing of the Sargasso Sea (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-04-07
    Description: We have applied "whole-genome shotgun sequencing" to microbial populations collected en masse on tangential flow and impact filters from seawater samples collected from the Sargasso Sea near Bermuda. A total of 1.045 billion base pairs of nonredundant sequence was generated, annotated, and analyzed to elucidate the gene content, diversity, and relative abundance of the organisms within these environmental samples. These data are estimated to derive from at least 1800 genomic species based on sequence relatedness, including 148 previously unknown bacterial phylotypes. We have identified over 1.2 million previously unknown genes represented in these samples, including more than 782 new rhodopsin-like photoreceptors. Variation in species present and stoichiometry suggests substantial oceanic microbial diversity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Venter, J Craig -- Remington, Karin -- Heidelberg, John F -- Halpern, Aaron L -- Rusch, Doug -- Eisen, Jonathan A -- Wu, Dongying -- Paulsen, Ian -- Nelson, Karen E -- Nelson, William -- Fouts, Derrick E -- Levy, Samuel -- Knap, Anthony H -- Lomas, Michael W -- Nealson, Ken -- White, Owen -- Peterson, Jeremy -- Hoffman, Jeff -- Parsons, Rachel -- Baden-Tillson, Holly -- Pfannkoch, Cynthia -- Rogers, Yu-Hui -- Smith, Hamilton O -- New York, N.Y. -- Science. 2004 Apr 2;304(5667):66-74. Epub 2004 Mar 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Biological Energy Alternatives, 1901 Research Boulevard, Rockville, MD 20850, USA. jcventer@tcag.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15001713" target="_blank"〉PubMed〈/a〉
    Keywords: Archaea/*genetics ; Atlantic Ocean ; Bacteria/*genetics ; Bacteriophages/genetics ; Biodiversity ; Computational Biology ; Cyanobacteria/genetics/growth & development/metabolism ; *Ecosystem ; Eukaryotic Cells ; Genes, Archaeal ; Genes, Bacterial ; Genes, rRNA ; Genome, Archaeal ; *Genome, Bacterial ; *Genomics ; Molecular Sequence Data ; Photosynthesis ; Phylogeny ; Plasmids ; Rhodopsin/genetics ; Rhodopsins, Microbial ; Seawater/*microbiology ; *Sequence Analysis, DNA ; Water Microbiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    The structure and receptor binding properties of the 1918 influenza hemagglutinin (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-02-07
    Description: The 1918 influenza pandemic resulted in about 20 million deaths. This enormous impact, coupled with renewed interest in emerging infections, makes characterization of the virus involved a priority. Receptor binding, the initial event in virus infection, is a major determinant of virus transmissibility that, for influenza viruses, is mediated by the hemagglutinin (HA) membrane glycoprotein. We have determined the crystal structures of the HA from the 1918 virus and two closely related HAs in complex with receptor analogs. They explain how the 1918 HA, while retaining receptor binding site amino acids characteristic of an avian precursor HA, is able to bind human receptors and how, as a consequence, the virus was able to spread in the human population.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gamblin, S J -- Haire, L F -- Russell, R J -- Stevens, D J -- Xiao, B -- Ha, Y -- Vasisht, N -- Steinhauer, D A -- Daniels, R S -- Elliot, A -- Wiley, D C -- Skehel, J J -- AI-13654/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2004 Mar 19;303(5665):1838-42. Epub 2004 Feb 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council (MRC) National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14764886" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Birds ; Crystallography, X-Ray ; Hemagglutinin Glycoproteins, Influenza Virus/*chemistry/*metabolism ; History, 20th Century ; Humans ; Hydrogen Bonding ; Influenza A virus/*immunology/metabolism/pathogenicity ; Influenza, Human/epidemiology/history/*virology ; Membrane Glycoproteins/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Tertiary ; Receptors, Virus/*metabolism ; Sequence Alignment ; Sialic Acids/metabolism ; Species Specificity ; Swine
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Discovery of symbiotic nitrogen-fixing cyanobacteria in corals (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-18
    Description: Colonies of the Caribbean coral Montastraea cavernosa exhibit a solar-stimulated orange-red fluorescence that is spectrally similar to a variety of fluorescent proteins expressed by corals. The source of this fluorescence is phycoerythrin in unicellular, nonheterocystis, symbiotic cyanobacteria within the host cells of the coral. The cyanobacteria coexist with the symbiotic dinoflagellates (zooxanthellae) of the coral and express the nitrogen-fixing enzyme nitrogenase. The presence of this prokaryotic symbiont in a nitrogen-limited zooxanthellate coral suggests that nitrogen fixation may be an important source of this limiting element for the symbiotic association.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lesser, Michael P -- Mazel, Charles H -- Gorbunov, Maxim Y -- Falkowski, Paul G -- New York, N.Y. -- Science. 2004 Aug 13;305(5686):997-1000.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology and Center for Marine Biology, University of New Hampshire, Durham, NH 03824, USA. mpl@cisunix.unh.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15310901" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anthozoa/*microbiology/physiology ; Cyanobacteria/genetics/isolation & purification/*physiology/ultrastructure ; Dinoflagellida/isolation & purification/physiology ; Fluorescence ; Microscopy, Fluorescence ; Molecular Sequence Data ; *Nitrogen Fixation ; Nitrogenase/genetics/metabolism ; Organelles/ultrastructure ; Phycoerythrin/metabolism ; *Symbiosis ; Thylakoids/ultrastructure
    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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  • 8
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    Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 A (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-09-14
    Description: The first structure of an ammonia channel from the Amt/MEP/Rh protein superfamily, determined to 1.35 angstrom resolution, shows it to be a channel that spans the membrane 11 times. Two structurally similar halves span the membrane with opposite polarity. Structures with and without ammonia or methyl ammonia show a vestibule that recruits NH4+/NH3, a binding site for NH4+, and a 20 angstrom-long hydrophobic channel that lowers the NH4+ pKa to below 6 and conducts NH3. Favorable interactions for NH3 are seen within the channel and use conserved histidines. Reconstitution of AmtB into vesicles shows that AmtB conducts uncharged NH3.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Khademi, Shahram -- O'Connell, Joseph 3rd -- Remis, Jonathan -- Robles-Colmenares, Yaneth -- Miercke, Larry J W -- Stroud, Robert M -- GM24485/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Sep 10;305(5690):1587-94.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, S412C Genentech Hall, University of California-San Francisco, 600 16th Street, San Francisco, CA 94143-2240, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15361618" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Ammonia/*metabolism ; Binding Sites ; Biological Transport ; Cation Transport Proteins/*chemistry/genetics/metabolism ; Cell Membrane/chemistry ; Crystallization ; Crystallography, X-Ray ; Escherichia coli/*chemistry/metabolism ; Escherichia coli Proteins/*chemistry/genetics/metabolism ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; Liposomes ; Membrane Potentials ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Quaternary Ammonium Compounds/metabolism ; Rh-Hr Blood-Group System/chemistry/metabolism ; Sequence Alignment ; Water/chemistry/metabolism
    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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  • 9
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    Basis for structural diversity in homologous RNAs (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-02
    Description: Large RNA molecules, such as ribozymes, fold with well-defined tertiary structures that are important for their activity. There are many instances of ribozymes with identical function but differences in their secondary structures, suggesting alternative tertiary folds. Here, we report a crystal structure of the 161-nucleotide specificity domain of an A-type ribonuclease P that differs in secondary and tertiary structure from the specificity domain of a B-type molecule. Despite the differences, the cores of the domains have similar three-dimensional structure. Remarkably, the similar geometry of the cores is stabilized by a different set of interactions involving distinct auxiliary elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krasilnikov, Andrey S -- Xiao, Yinghua -- Pan, Tao -- Mondragon, Alfonso -- New York, N.Y. -- Science. 2004 Oct 1;306(5693):104-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15459389" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Catalytic Domain ; Conserved Sequence ; Crystallography, X-Ray ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Phylogeny ; RNA Precursors/chemistry/metabolism ; RNA, Bacterial/*chemistry/metabolism ; RNA, Transfer/chemistry/metabolism ; Ribonuclease P/*chemistry/metabolism ; Ribonucleotides/chemistry/metabolism ; Thermus thermophilus/*chemistry/enzymology
    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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  • 10
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    Discovery and directed evolution of a glyphosate tolerance gene (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-05-25
    Description: The herbicide glyphosate is effectively detoxified by N-acetylation. We screened a collection of microbial isolates and discovered enzymes exhibiting glyphosate N-acetyltransferase (GAT) activity. Kinetic properties of the discovered enzymes were insufficient to confer glyphosate tolerance to transgenic organisms. Eleven iterations of DNA shuffling improved enzyme efficiency by nearly four orders of magnitude from 0.87 mM-1 min-1 to 8320 mM-1 min-1. From the fifth iteration and beyond, GAT enzymes conferred increasing glyphosate tolerance to Escherichia coli, Arabidopsis, tobacco, and maize. Glyphosate acetylation provides an alternative strategy for supporting glyphosate use on crops.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castle, Linda A -- Siehl, Daniel L -- Gorton, Rebecca -- Patten, Phillip A -- Chen, Yong Hong -- Bertain, Sean -- Cho, Hyeon-Je -- Duck, Nicholas -- Wong, James -- Liu, Donglong -- Lassner, Michael W -- New York, N.Y. -- Science. 2004 May 21;304(5674):1151-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Verdia, Inc. Redwood City, CA 94063, USA. linda.castle@verdiainc.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15155947" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Acetyltransferases/chemistry/*genetics/metabolism ; Amino Acid Sequence ; Bacillus/enzymology ; Catalysis ; *DNA Shuffling ; *Directed Molecular Evolution ; Drug Resistance ; Escherichia coli/genetics ; Gene Library ; Genetic Variation ; Glycine/*analogs & derivatives/metabolism/*toxicity ; Herbicides/metabolism/*toxicity ; Kinetics ; Molecular Sequence Data ; Mutagenesis ; *Plants, Genetically Modified/drug effects/genetics ; Recombinant Proteins/metabolism ; Recombination, Genetic ; Tobacco/drug effects/genetics/growth & development ; Transformation, Genetic ; Zea mays/drug effects/genetics/growth & development
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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