A second, non‐canonical RNA‐dependent RNA polymerase in SARS Coronavirus
Identifieur interne : 001177 ( Pmc/Checkpoint ); précédent : 001176; suivant : 001178A second, non‐canonical RNA‐dependent RNA polymerase in SARS Coronavirus
Auteurs : Isabelle Imbert ; Jean-Claude Guillemot ; Jean-Marie Bourhis ; Cécile Bussetta ; Bruno Coutard ; Marie-Pierre Egloff ; François Ferron ; Alexander E. Gorbalenya ; Bruno CanardSource :
- The EMBO Journal [ 0261-4189 ] ; 2006.
Abstract
In (+) RNA coronaviruses, replication and transcription of the giant ∼30 kb genome to produce genome‐ and subgenome‐size RNAs of both polarities are mediated by a cognate membrane‐bound enzymatic complex. Its RNA‐dependent RNA polymerase (RdRp) activity appears to be supplied by non‐structural protein 12 (nsp12) that includes an RdRp domain conserved in all RNA viruses. Using SARS coronavirus, we now show that coronaviruses uniquely encode a second RdRp residing in nsp8. This protein strongly prefers the internal 5′‐(G/U)CC‐3′ trinucleotides on RNA templates to initiate the synthesis of complementary oligonucleotides of <6 residues in a reaction whose fidelity is relatively low. Distant structural homology between the C‐terminal domain of nsp8 and the catalytic palm subdomain of RdRps of RNA viruses suggests a common origin of the two coronavirus RdRps, which however may have evolved different sets of catalytic residues. A parallel between the nsp8 RdRp and cellular DNA‐dependent RNA primases is drawn to propose that the nsp8 RdRp produces primers utilized by the primer‐dependent nsp12 RdRp.
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DOI: 10.1038/sj.emboj.7601368
PubMed: 17024178
PubMed Central: 1618104
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Gorbalenya</name><affiliation><nlm:aff id="embj7601368-aff-0002"></nlm:aff></affiliation></author><author><name sortKey="Canard, Bruno" sort="Canard, Bruno" uniqKey="Canard B" first="Bruno" last="Canard">Bruno Canard</name><affiliation><nlm:aff id="embj7601368-aff-0001"></nlm:aff></affiliation></author></analytic><series><title level="j">The EMBO Journal</title><idno type="ISSN">0261-4189</idno><idno type="eISSN">1460-2075</idno><imprint><date when="2006">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>In (+) RNA coronaviruses, replication and transcription of the giant ∼30 kb genome to produce genome‐ and subgenome‐size RNAs of both polarities are mediated by a cognate membrane‐bound enzymatic complex. Its RNA‐dependent RNA polymerase (RdRp) activity appears to be supplied by non‐structural protein 12 (nsp12) that includes an RdRp domain conserved in all RNA viruses. Using SARS coronavirus, we now show that coronaviruses uniquely encode a second RdRp residing in nsp8. This protein strongly prefers the internal 5′‐(G/U)CC‐3′ trinucleotides on RNA templates to initiate the synthesis of complementary oligonucleotides of <6 residues in a reaction whose fidelity is relatively low. Distant structural homology between the C‐terminal domain of nsp8 and the catalytic palm subdomain of RdRps of RNA viruses suggests a common origin of the two coronavirus RdRps, which however may have evolved different sets of catalytic residues. A parallel between the nsp8 RdRp and cellular DNA‐dependent RNA primases is drawn to propose that the nsp8 RdRp produces primers utilized by the primer‐dependent nsp12 RdRp.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct></listBibl></div1></back></TEI><pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">EMBO J</journal-id><journal-id journal-id-type="iso-abbrev">EMBO J</journal-id><journal-id journal-id-type="doi">10.1002/(ISSN)1460-2075</journal-id><journal-id journal-id-type="publisher-id">EMBJ</journal-id><journal-id journal-id-type="hwp">embojnl</journal-id><journal-title-group><journal-title>The EMBO Journal</journal-title></journal-title-group><issn pub-type="ppub">0261-4189</issn><issn pub-type="epub">1460-2075</issn><publisher><publisher-name>John Wiley & Sons, Ltd</publisher-name><publisher-loc>Chichester, UK</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">17024178</article-id><article-id pub-id-type="pmc">1618104</article-id><article-id pub-id-type="doi">10.1038/sj.emboj.7601368</article-id><article-id pub-id-type="publisher-id">EMBJ7601368</article-id><article-categories><subj-group subj-group-type="overline"><subject>Article</subject></subj-group><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>A second, non‐canonical RNA‐dependent RNA polymerase in SARS Coronavirus</article-title><alt-title alt-title-type="right-running-head">Sequence‐specific RNA‐dependent RNA polymerase</alt-title></title-group><contrib-group><contrib id="embj7601368-cr-0001" contrib-type="author"><name><surname>Imbert</surname><given-names>Isabelle</given-names></name><xref ref-type="aff" rid="embj7601368-aff-0001"><sup>1</sup></xref></contrib><contrib id="embj7601368-cr-0002" contrib-type="author"><name><surname>Guillemot</surname><given-names>Jean‐Claude</given-names></name><xref ref-type="aff" rid="embj7601368-aff-0001"><sup>1</sup></xref></contrib><contrib id="embj7601368-cr-0003" contrib-type="author"><name><surname>Bourhis</surname><given-names>Jean‐Marie</given-names></name><xref ref-type="aff" rid="embj7601368-aff-0001"><sup>1</sup></xref></contrib><contrib id="embj7601368-cr-0004" contrib-type="author"><name><surname>Bussetta</surname><given-names>Cécile</given-names></name><xref ref-type="aff" rid="embj7601368-aff-0001"><sup>1</sup></xref></contrib><contrib id="embj7601368-cr-0005" contrib-type="author"><name><surname>Coutard</surname><given-names>Bruno</given-names></name><xref ref-type="aff" rid="embj7601368-aff-0001"><sup>1</sup></xref></contrib><contrib id="embj7601368-cr-0006" contrib-type="author"><name><surname>Egloff</surname><given-names>Marie‐Pierre</given-names></name><xref ref-type="aff" rid="embj7601368-aff-0001"><sup>1</sup></xref></contrib><contrib id="embj7601368-cr-0007" contrib-type="author"><name><surname>Ferron</surname><given-names>François</given-names></name><xref ref-type="aff" rid="embj7601368-aff-0001"><sup>1</sup></xref><xref ref-type="author-notes" rid="embj7601368-note-0001"><sup>†</sup></xref></contrib><contrib id="embj7601368-cr-0008" contrib-type="author"><name><surname>Gorbalenya</surname><given-names>Alexander E</given-names></name><xref ref-type="aff" rid="embj7601368-aff-0002"><sup>2</sup></xref></contrib><contrib id="embj7601368-cr-0009" contrib-type="author" corresp="yes"><name><surname>Canard</surname><given-names>Bruno</given-names></name><xref ref-type="aff" rid="embj7601368-aff-0001"><sup>1</sup></xref></contrib></contrib-group><aff id="embj7601368-aff-0001"><label><sup>1</sup></label><institution>Centre National de la Recherche Scientifique and Universités d'Aix‐Marseille I et II, UMR 6098, Architecture et Fonction des Macromolécules Biologiques, Ecole Supérieure d'Ingénieurs de Luminy‐Case 925</institution><city>Marseille Cedex</city><country country="FR">France</country></aff><aff id="embj7601368-aff-0002"><label><sup>2</sup></label><institution>Molecular Virology Laboratory, Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center</institution><city>Leiden</city><country country="NL">The Netherlands</country></aff><author-notes><corresp id="correspondenceTo"><label>*</label>Corresponding author. Centre National de la Recherche Scientifique and Universités d'Aix‐Marseille I et II, UMR 6098, Architecture et Fonction des Macromolécules Biologiques, Ecole Supérieure d'Ingénieurs de Luminy‐Case 925, 163 Avenue de Luminy, 13288 Marseille Cedex 9, France. Tel.: +33 491 82 86 44; Fax: +33 491 82 86 46; E-mail: <email>Bruno.Canard@afmb.univ-mrs.fr</email> or <email>bruno@afmb.univ-mrs.fr</email></corresp><fn id="embj7601368-note-0001" fn-type="present-address"><label>†</label><p>Present address: Boston Biomedical Research Institute, 64, grove St., Watertown, 02472, MA, USA</p></fn></author-notes><pub-date pub-type="ppub"><day>18</day><month>10</month><year>2006</year></pub-date><pub-date pub-type="epub"><day>05</day><month>10</month><year>2006</year></pub-date><volume>25</volume><issue>20</issue><issue-id pub-id-type="doi">10.1002/emboj.v25.20</issue-id><fpage>4933</fpage><lpage>4942</lpage><history><date date-type="received"><day>10</day><month>3</month><year>2006</year></date><date date-type="accepted"><day>01</day><month>9</month><year>2006</year></date></history><permissions><pmc-comment> Copyright © 2013 Wiley Periodicals, Inc </pmc-comment>
<copyright-statement content-type="article-copyright">Copyright © 2006 European Molecular Biology Organization</copyright-statement><license><license-p>This article is being made freely available through PubMed Central as part of the COVID-19 public health emergency response. It can be used for unrestricted research re-use and analysis in any form or by any means with acknowledgement of the original source, for the duration of the public health emergency.</license-p></license></permissions><self-uri content-type="pdf" xlink:href="file:EMBJ-25-4933.pdf"></self-uri><abstract><p>In (+) RNA coronaviruses, replication and transcription of the giant ∼30 kb genome to produce genome‐ and subgenome‐size RNAs of both polarities are mediated by a cognate membrane‐bound enzymatic complex. Its RNA‐dependent RNA polymerase (RdRp) activity appears to be supplied by non‐structural protein 12 (nsp12) that includes an RdRp domain conserved in all RNA viruses. Using SARS coronavirus, we now show that coronaviruses uniquely encode a second RdRp residing in nsp8. This protein strongly prefers the internal 5′‐(G/U)CC‐3′ trinucleotides on RNA templates to initiate the synthesis of complementary oligonucleotides of <6 residues in a reaction whose fidelity is relatively low. Distant structural homology between the C‐terminal domain of nsp8 and the catalytic palm subdomain of RdRps of RNA viruses suggests a common origin of the two coronavirus RdRps, which however may have evolved different sets of catalytic residues. A parallel between the nsp8 RdRp and cellular DNA‐dependent RNA primases is drawn to propose that the nsp8 RdRp produces primers utilized by the primer‐dependent nsp12 RdRp.</p></abstract><kwd-group kwd-group-type="author-generated"><kwd id="embj7601368-kwd-0001">coronavirus</kwd><kwd id="embj7601368-kwd-0002">polymerase</kwd><kwd id="embj7601368-kwd-0003">replication</kwd><kwd id="embj7601368-kwd-0004">RNA</kwd><kwd id="embj7601368-kwd-0005">SARS</kwd></kwd-group><kwd-group kwd-group-type="subject-categories"><title>Subject Categories</title><kwd>DNA Replication, Repair & Recombination</kwd><kwd>Microbiology, Virology & Host Pathogen Interaction</kwd></kwd-group><counts><page-count count="10"></page-count></counts><custom-meta-group><custom-meta><meta-name>source-schema-version-number</meta-name><meta-value>2.0</meta-value></custom-meta><custom-meta><meta-name>cover-date</meta-name><meta-value>October 18, 2006</meta-value></custom-meta><custom-meta><meta-name>details-of-publishers-convertor</meta-name><meta-value>Converter:WILEY_ML3GV2_TO_JATSPMC version:5.8.0 mode:remove_FC converted:15.04.2020</meta-value></custom-meta></custom-meta-group></article-meta></front></pmc><affiliations><list></list><tree><noCountry><name sortKey="Bourhis, Jean Arie" sort="Bourhis, Jean Arie" uniqKey="Bourhis J" first="Jean-Marie" last="Bourhis">Jean-Marie Bourhis</name><name sortKey="Bussetta, Cecile" sort="Bussetta, Cecile" uniqKey="Bussetta C" first="Cécile" last="Bussetta">Cécile Bussetta</name><name sortKey="Canard, Bruno" sort="Canard, Bruno" uniqKey="Canard B" first="Bruno" last="Canard">Bruno Canard</name><name sortKey="Coutard, Bruno" sort="Coutard, Bruno" uniqKey="Coutard B" first="Bruno" last="Coutard">Bruno Coutard</name><name sortKey="Egloff, Marie Ierre" sort="Egloff, Marie Ierre" uniqKey="Egloff M" first="Marie-Pierre" last="Egloff">Marie-Pierre Egloff</name><name sortKey="Ferron, Francois" sort="Ferron, Francois" uniqKey="Ferron F" first="François" last="Ferron">François Ferron</name><name sortKey="Gorbalenya, Alexander E" sort="Gorbalenya, Alexander E" uniqKey="Gorbalenya A" first="Alexander E" last="Gorbalenya">Alexander E. Gorbalenya</name><name sortKey="Guillemot, Jean Laude" sort="Guillemot, Jean Laude" uniqKey="Guillemot J" first="Jean-Claude" last="Guillemot">Jean-Claude Guillemot</name><name sortKey="Imbert, Isabelle" sort="Imbert, Isabelle" uniqKey="Imbert I" first="Isabelle" last="Imbert">Isabelle Imbert</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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