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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The Severe Acute Respiratory Syndrome Coronavirus Nsp15 Protein Is an Endoribonuclease That Prefers Manganese as a Cofactor</title><author><name sortKey="Bhardwaj, Kanchan" sort="Bhardwaj, Kanchan" uniqKey="Bhardwaj K" first="Kanchan" last="Bhardwaj">Kanchan Bhardwaj</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas</nlm:aff></affiliation></author><author><name sortKey="Guarino, Linda" sort="Guarino, Linda" uniqKey="Guarino L" first="Linda" last="Guarino">Linda Guarino</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas</nlm:aff></affiliation></author><author><name sortKey="Kao, C Cheng" sort="Kao, C Cheng" uniqKey="Kao C" first="C. Cheng" last="Kao">C. Cheng Kao</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">15507608</idno><idno type="pmc">525082</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC525082</idno><idno type="RBID">PMC:525082</idno><idno type="doi">10.1128/JVI.78.22.12218-12224.2004</idno><date when="2004">2004</date><idno type="wicri:Area/Pmc/Corpus">000686</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000686</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">The Severe Acute Respiratory Syndrome Coronavirus Nsp15 Protein Is an Endoribonuclease That Prefers Manganese as a Cofactor</title><author><name sortKey="Bhardwaj, Kanchan" sort="Bhardwaj, Kanchan" uniqKey="Bhardwaj K" first="Kanchan" last="Bhardwaj">Kanchan Bhardwaj</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas</nlm:aff></affiliation></author><author><name sortKey="Guarino, Linda" sort="Guarino, Linda" uniqKey="Guarino L" first="Linda" last="Guarino">Linda Guarino</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas</nlm:aff></affiliation></author><author><name sortKey="Kao, C Cheng" sort="Kao, C Cheng" uniqKey="Kao C" first="C. Cheng" last="Kao">C. Cheng Kao</name><affiliation><nlm:aff id="aff0">Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas</nlm:aff></affiliation></author></analytic><series><title level="j">Journal of Virology</title><idno type="ISSN">0022-538X</idno><idno type="eISSN">1098-5514</idno><imprint><date when="2004">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Nonstructural protein 15 (Nsp15) of the severe acute respiratory syndrome coronavirus (SARS-CoV) produced in <italic>Escherichia coli</italic> has endoribonuclease activity that preferentially cleaved 5′ of uridylates of RNAs. Blocking either the 5′ or 3′ terminus did not affect cleavage. Double- and single-stranded RNAs were both substrates for Nsp15 but with different kinetics for cleavage. Mn<sup>2+</sup> at 2 to 10 mM was needed for optimal endoribonuclease activity, but Mg<sup>2+</sup> and several other divalent metals were capable of supporting only a low level of activity. Concentrations of Mn<sup>2+</sup> needed for endoribonuclease activity induced significant conformation change(s) in the protein, as measured by changes in tryptophan fluorescence. A similar endoribonucleolytic activity was detected for the orthologous protein from another coronavirus, demonstrating that the endoribonuclease activity of Nsp15 may be common to coronaviruses. This work presents an initial biochemical characterization of a novel coronavirus endoribonuclease.</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 Virol</journal-id><journal-id journal-id-type="publisher-id">jvi</journal-id><journal-title>Journal of Virology</journal-title><issn pub-type="ppub">0022-538X</issn><issn pub-type="epub">1098-5514</issn><publisher><publisher-name>American Society for Microbiology</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">15507608</article-id><article-id pub-id-type="pmc">525082</article-id><article-id pub-id-type="publisher-id">0929-04</article-id><article-id pub-id-type="doi">10.1128/JVI.78.22.12218-12224.2004</article-id><article-categories><subj-group subj-group-type="heading"><subject>Replication</subject></subj-group></article-categories><title-group><article-title>The Severe Acute Respiratory Syndrome Coronavirus Nsp15 Protein Is an Endoribonuclease That Prefers Manganese as a Cofactor</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Bhardwaj</surname><given-names>Kanchan</given-names></name><xref ref-type="aff" rid="aff0"></xref></contrib><contrib contrib-type="author"><name><surname>Guarino</surname><given-names>Linda</given-names></name><xref ref-type="aff" rid="aff0"></xref></contrib><contrib contrib-type="author"><name><surname>Kao</surname><given-names>C. Cheng</given-names></name><xref ref-type="aff" rid="aff0"></xref><xref ref-type="corresp" rid="cor1">*</xref></contrib></contrib-group><aff id="aff0">Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas</aff><author-notes><fn id="cor1"><label>*</label><p>Corresponding author. Mailing address: Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-2128. Phone: (979) 458-2235. Fax: (979) 845-9274. E-mail: <email>ckao@tamu.edu</email>.</p></fn></author-notes><pub-date pub-type="ppub"><month>11</month><year>2004</year></pub-date><volume>78</volume><issue>22</issue><fpage>12218</fpage><lpage>12224</lpage><history><date date-type="received"><day>23</day><month>4</month><year>2004</year></date><date date-type="accepted"><day>9</day><month>7</month><year>2004</year></date></history><copyright-statement>Copyright © 2004, American Society for Microbiology</copyright-statement><copyright-year>2004</copyright-year><abstract><p>Nonstructural protein 15 (Nsp15) of the severe acute respiratory syndrome coronavirus (SARS-CoV) produced in <italic>Escherichia coli</italic> has endoribonuclease activity that preferentially cleaved 5′ of uridylates of RNAs. Blocking either the 5′ or 3′ terminus did not affect cleavage. Double- and single-stranded RNAs were both substrates for Nsp15 but with different kinetics for cleavage. Mn<sup>2+</sup> at 2 to 10 mM was needed for optimal endoribonuclease activity, but Mg<sup>2+</sup> and several other divalent metals were capable of supporting only a low level of activity. Concentrations of Mn<sup>2+</sup> needed for endoribonuclease activity induced significant conformation change(s) in the protein, as measured by changes in tryptophan fluorescence. A similar endoribonucleolytic activity was detected for the orthologous protein from another coronavirus, demonstrating that the endoribonuclease activity of Nsp15 may be common to coronaviruses. This work presents an initial biochemical characterization of a novel coronavirus endoribonuclease.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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