Identification of Lethal Mutations in Yeast Threonyl-tRNA Synthetase Revealing Critical Residues in Its Human Homolog*
Identifieur interne : 000476 ( Pmc/Curation ); précédent : 000475; suivant : 000477Identification of Lethal Mutations in Yeast Threonyl-tRNA Synthetase Revealing Critical Residues in Its Human Homolog*
Auteurs : Zhi-Rong Ruan ; Zhi-Peng Fang ; Qing Ye ; Hui-Yan Lei ; Gilbert Eriani [France] ; Xiao-Long Zhou ; En-Duo WangSource :
- The Journal of Biological Chemistry [ 0021-9258 ] ; 2014.
Abstract
Url:
DOI: 10.1074/jbc.M114.599886
PubMed: 25416776
PubMed Central: 4340410
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Identification of Lethal Mutations in Yeast Threonyl-tRNA Synthetase Revealing Critical Residues in Its Human Homolog<xref ref-type="fn" rid="FN1">*</xref></title><author><name sortKey="Ruan, Zhi Rong" sort="Ruan, Zhi Rong" uniqKey="Ruan Z" first="Zhi-Rong" last="Ruan">Zhi-Rong Ruan</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Fang, Zhi Peng" sort="Fang, Zhi Peng" uniqKey="Fang Z" first="Zhi-Peng" last="Fang">Zhi-Peng Fang</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Ye, Qing" sort="Ye, Qing" uniqKey="Ye Q" first="Qing" last="Ye">Qing Ye</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Lei, Hui Yan" sort="Lei, Hui Yan" uniqKey="Lei H" first="Hui-Yan" last="Lei">Hui-Yan Lei</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Eriani, Gilbert" sort="Eriani, Gilbert" uniqKey="Eriani G" first="Gilbert" last="Eriani">Gilbert Eriani</name><affiliation wicri:level="1"><nlm:aff id="aff3">Architecture et Réactivité de l'ARN, Université de Strasbourg, CNRS, Institut de Biologie Moléculaire et Cellulaire, 15 Rue René Descartes, 67084 Strasbourg, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Architecture et Réactivité de l'ARN, Université de Strasbourg, CNRS, Institut de Biologie Moléculaire et Cellulaire, 15 Rue René Descartes, 67084 Strasbourg</wicri:regionArea></affiliation></author><author><name sortKey="Zhou, Xiao Long" sort="Zhou, Xiao Long" uniqKey="Zhou X" first="Xiao-Long" last="Zhou">Xiao-Long Zhou</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Wang, En Duo" sort="Wang, En Duo" uniqKey="Wang E" first="En-Duo" last="Wang">En-Duo Wang</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">25416776</idno><idno type="pmc">4340410</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4340410</idno><idno type="RBID">PMC:4340410</idno><idno type="doi">10.1074/jbc.M114.599886</idno><date when="2014">2014</date><idno type="wicri:Area/Pmc/Corpus">000479</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000479</idno><idno type="wicri:Area/Pmc/Curation">000476</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000476</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Identification of Lethal Mutations in Yeast Threonyl-tRNA Synthetase Revealing Critical Residues in Its Human Homolog<xref ref-type="fn" rid="FN1">*</xref></title><author><name sortKey="Ruan, Zhi Rong" sort="Ruan, Zhi Rong" uniqKey="Ruan Z" first="Zhi-Rong" last="Ruan">Zhi-Rong Ruan</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Fang, Zhi Peng" sort="Fang, Zhi Peng" uniqKey="Fang Z" first="Zhi-Peng" last="Fang">Zhi-Peng Fang</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Ye, Qing" sort="Ye, Qing" uniqKey="Ye Q" first="Qing" last="Ye">Qing Ye</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Lei, Hui Yan" sort="Lei, Hui Yan" uniqKey="Lei H" first="Hui-Yan" last="Lei">Hui-Yan Lei</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Eriani, Gilbert" sort="Eriani, Gilbert" uniqKey="Eriani G" first="Gilbert" last="Eriani">Gilbert Eriani</name><affiliation wicri:level="1"><nlm:aff id="aff3">Architecture et Réactivité de l'ARN, Université de Strasbourg, CNRS, Institut de Biologie Moléculaire et Cellulaire, 15 Rue René Descartes, 67084 Strasbourg, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Architecture et Réactivité de l'ARN, Université de Strasbourg, CNRS, Institut de Biologie Moléculaire et Cellulaire, 15 Rue René Descartes, 67084 Strasbourg</wicri:regionArea></affiliation></author><author><name sortKey="Zhou, Xiao Long" sort="Zhou, Xiao Long" uniqKey="Zhou X" first="Xiao-Long" last="Zhou">Xiao-Long Zhou</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Wang, En Duo" sort="Wang, En Duo" uniqKey="Wang E" first="En-Duo" last="Wang">En-Duo Wang</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author></analytic><series><title level="j">The Journal of Biological Chemistry</title><idno type="ISSN">0021-9258</idno><idno type="eISSN">1083-351X</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><bold>Background:</bold> Eukaryotic ThrRSs exhibit four structural domains similar to bacterial ThrRSs and evolve a eukaryote-specific N-terminal extension domain.</p><p><bold>Results:</bold> Essential roles of 12 crucial residues in aminoacylation and editing reactions were revealed.</p><p><bold>Conclusion:</bold> The identified critical residues affected activities of ThrRS in various manners.</p><p><bold>Significance:</bold> We elucidated the synthetic and editing functions of selected residues and confirmed the functional consistency between yeast and human ThrRSs.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Biol Chem</journal-id><journal-id journal-id-type="iso-abbrev">J. Biol. Chem</journal-id><journal-id journal-id-type="hwp">jbc</journal-id><journal-id journal-id-type="pmc">jbc</journal-id><journal-id journal-id-type="publisher-id">JBC</journal-id><journal-title-group><journal-title>The Journal of Biological Chemistry</journal-title></journal-title-group><issn pub-type="ppub">0021-9258</issn><issn pub-type="epub">1083-351X</issn><publisher><publisher-name>American Society for Biochemistry and Molecular Biology</publisher-name><publisher-loc>9650 Rockville Pike, Bethesda, MD 20814, U.S.A.</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">25416776</article-id><article-id pub-id-type="pmc">4340410</article-id><article-id pub-id-type="publisher-id">M114.599886</article-id><article-id pub-id-type="doi">10.1074/jbc.M114.599886</article-id><article-categories><subj-group subj-group-type="heading"><subject>Enzymology</subject></subj-group></article-categories><title-group><article-title>Identification of Lethal Mutations in Yeast Threonyl-tRNA Synthetase Revealing Critical Residues in Its Human Homolog<xref ref-type="fn" rid="FN1">*</xref></article-title><alt-title alt-title-type="short">Selected Lethal Mutations in Threonyl-tRNA Synthetase</alt-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Ruan</surname><given-names>Zhi-Rong</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref></contrib><contrib contrib-type="author"><name><surname>Fang</surname><given-names>Zhi-Peng</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref></contrib><contrib contrib-type="author"><name><surname>Ye</surname><given-names>Qing</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref></contrib><contrib contrib-type="author"><name><surname>Lei</surname><given-names>Hui-Yan</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref></contrib><contrib contrib-type="author"><name><surname>Eriani</surname><given-names>Gilbert</given-names></name><xref ref-type="aff" rid="aff3"><sup>§</sup></xref></contrib><contrib contrib-type="author"><name><surname>Zhou</surname><given-names>Xiao-Long</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref><xref ref-type="corresp" rid="cor1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Wang</surname><given-names>En-Duo</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref><xref ref-type="aff" rid="aff2"><sup>¶</sup></xref><xref ref-type="corresp" rid="cor2"><sup>2</sup></xref></contrib><aff id="aff1">From the<label>‡</label>Center for RNA Research, State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, China,</aff><aff id="aff2">the<label>¶</label>School of Life Science and Technology, ShanghaiTech University, 320 Yue Yang Road, Shanghai 200031, China, and</aff><aff id="aff3"><label>§</label>Architecture et Réactivité de l'ARN, Université de Strasbourg, CNRS, Institut de Biologie Moléculaire et Cellulaire, 15 Rue René Descartes, 67084 Strasbourg, France</aff></contrib-group><author-notes><corresp id="cor1"><label>1</label> To whom correspondence may be addressed. Tel.: <phone>86-21-5492-1241</phone>; Fax: <fax>86-21-5492-1011</fax>; E-mail: <email>xlzhou@sibcb.ac.cn</email>.</corresp><corresp id="cor2"><label>2</label> To whom correspondence may be addressed. Tel.: <phone>86-21-5492-1241</phone>; Fax: <fax>86-21-5492-1011</fax>; E-mail: <email>edwang@sibcb.ac.cn</email>.</corresp></author-notes><pub-date pub-type="ppub"><day>16</day><month>1</month><year>2015</year></pub-date><pub-date pub-type="epub"><day>21</day><month>11</month><year>2014</year></pub-date><volume>290</volume><issue>3</issue><fpage>1664</fpage><lpage>1678</lpage><history><date date-type="received"><day>12</day><month>8</month><year>2014</year></date><date date-type="rev-recd"><day>3</day><month>11</month><year>2014</year></date></history><permissions><copyright-statement>© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.</copyright-statement><copyright-year>2015</copyright-year></permissions><self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zbc00315001664.pdf"></self-uri><abstract abstract-type="teaser"><p><bold>Background:</bold> Eukaryotic ThrRSs exhibit four structural domains similar to bacterial ThrRSs and evolve a eukaryote-specific N-terminal extension domain.</p><p><bold>Results:</bold> Essential roles of 12 crucial residues in aminoacylation and editing reactions were revealed.</p><p><bold>Conclusion:</bold> The identified critical residues affected activities of ThrRS in various manners.</p><p><bold>Significance:</bold> We elucidated the synthetic and editing functions of selected residues and confirmed the functional consistency between yeast and human ThrRSs.</p></abstract><abstract><p>Aminoacyl-tRNA synthetases (aaRSs) are a group of ancient enzymes catalyzing aminoacylation and editing reactions for protein biosynthesis. Increasing evidence suggests that these critical enzymes are often associated with mammalian disorders. Therefore, complete determination of the enzymes functions is essential for informed diagnosis and treatment. Here, we show that a yeast knock-out strain for the threonyl-tRNA synthetase (ThrRS) gene is an excellent platform for such an investigation. <italic>Saccharomyces cerevisiae</italic> ThrRS has a unique modular structure containing four structural domains and a eukaryote-specific N-terminal extension. Using randomly mutated libraries of the ThrRS gene (<italic>thrS</italic>) and a genetic screen, a set of loss-of-function mutants were identified. The mutations affected the synthetic and editing activities and influenced the dimer interface. The results also highlighted the role of the N-terminal extension for enzymatic activity and protein stability. To gain insights into the pathological mechanisms induced by mutated aaRSs, we systematically introduced the loss-of-function mutations into the human cytoplasmic ThrRS gene. All mutations induced similar detrimental effects, showing that the yeast model could be used to study pathology-associated point mutations in mammalian aaRSs.</p></abstract><kwd-group><kwd>Aminoacyl tRNA Synthetase</kwd><kwd>Mutagenesis</kwd><kwd>Protein Structure</kwd><kwd>Transfer RNA (tRNA)</kwd><kwd>Translation</kwd><kwd>Aminoacylation, Editing</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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