A second, non-canonical RNA-dependent RNA polymerase in SARS coronavirus.
Identifieur interne : 002070 ( PubMed/Corpus ); précédent : 002069; suivant : 002071A 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.
English descriptors
- KwdEn :
- Amino Acid Sequence, Catalytic Domain (genetics), Models, Molecular, Molecular Sequence Data, Protein Structure, Tertiary (genetics), RNA Replicase (chemistry), RNA Replicase (genetics), RNA Replicase (metabolism), RNA, Viral (biosynthesis), RNA, Viral (chemistry), RNA, Viral (genetics), SARS Virus (chemistry), SARS Virus (enzymology), SARS Virus (genetics), Viral Proteins (chemistry), Viral Proteins (genetics), Viral Proteins (metabolism).
- MESH :
- chemical , biosynthesis : RNA, Viral.
- chemical , chemistry : RNA Replicase, RNA, Viral, Viral Proteins.
- chemistry : SARS Virus.
- enzymology : SARS Virus.
- genetics : Catalytic Domain, Protein Structure, Tertiary, RNA Replicase, RNA, Viral, SARS Virus, Viral Proteins.
- chemical , metabolism : RNA Replicase, Viral Proteins.
- Amino Acid Sequence, Models, Molecular, Molecular Sequence Data.
Abstract
In (+) RNA coronaviruses, replication and transcription of the giant approximately 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.
DOI: 10.1038/sj.emboj.7601368
PubMed: 17024178
Links to Exploration step
pubmed:17024178Le document en format XML
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Gorbalenya</name></author><author><name sortKey="Canard, Bruno" sort="Canard, Bruno" uniqKey="Canard B" first="Bruno" last="Canard">Bruno Canard</name></author></analytic><series><title level="j">The EMBO journal</title><idno type="ISSN">0261-4189</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Catalytic Domain (genetics)</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Structure, Tertiary (genetics)</term><term>RNA Replicase (chemistry)</term><term>RNA Replicase (genetics)</term><term>RNA Replicase (metabolism)</term><term>RNA, Viral (biosynthesis)</term><term>RNA, Viral (chemistry)</term><term>RNA, Viral (genetics)</term><term>SARS Virus (chemistry)</term><term>SARS Virus (enzymology)</term><term>SARS Virus (genetics)</term><term>Viral Proteins (chemistry)</term><term>Viral Proteins (genetics)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>RNA, Viral</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>RNA Replicase</term><term>RNA, Viral</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Catalytic Domain</term><term>Protein Structure, Tertiary</term><term>RNA Replicase</term><term>RNA, Viral</term><term>SARS Virus</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>RNA Replicase</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Models, Molecular</term><term>Molecular Sequence Data</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In (+) RNA coronaviruses, replication and transcription of the giant approximately 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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17024178</PMID><DateCompleted><Year>2006</Year><Month>12</Month><Day>04</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0261-4189</ISSN><JournalIssue CitedMedium="Print"><Volume>25</Volume><Issue>20</Issue><PubDate><Year>2006</Year><Month>Oct</Month><Day>18</Day></PubDate></JournalIssue><Title>The EMBO journal</Title><ISOAbbreviation>EMBO J.</ISOAbbreviation></Journal><ArticleTitle>A second, non-canonical RNA-dependent RNA polymerase in SARS coronavirus.</ArticleTitle><Pagination><MedlinePgn>4933-42</MedlinePgn></Pagination><Abstract><AbstractText>In (+) RNA coronaviruses, replication and transcription of the giant approximately 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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Imbert</LastName><ForeName>Isabelle</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>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, Marseille Cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Guillemot</LastName><ForeName>Jean-Claude</ForeName><Initials>JC</Initials></Author><Author ValidYN="Y"><LastName>Bourhis</LastName><ForeName>Jean-Marie</ForeName><Initials>JM</Initials></Author><Author ValidYN="Y"><LastName>Bussetta</LastName><ForeName>Cécile</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Coutard</LastName><ForeName>Bruno</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Egloff</LastName><ForeName>Marie-Pierre</ForeName><Initials>MP</Initials></Author><Author ValidYN="Y"><LastName>Ferron</LastName><ForeName>François</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Gorbalenya</LastName><ForeName>Alexander E</ForeName><Initials>AE</Initials></Author><Author ValidYN="Y"><LastName>Canard</LastName><ForeName>Bruno</ForeName><Initials>B</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>10</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>EMBO 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