A second, non‐canonical RNA‐dependent RNA polymerase in SARS Coronavirus
Identifieur interne : 000202 ( France/Analysis ); précédent : 000201; suivant : 000203A second, non‐canonical RNA‐dependent RNA polymerase in SARS Coronavirus
Auteurs : Isabelle Imbert [France] ; Jean-Claude Guillemot [France] ; Jean-Marie Bourhis [France] ; Cécile Bussetta [France] ; Bruno Coutard [France] ; Marie-Pierre Egloff [France] ; François Ferron [France] ; Alexander E. Gorbalenya [Pays-Bas] ; Bruno Canard [France]Source :
- The EMBO Journal [ 0261-4189 ] ; 2006-10-18.
English descriptors
- Teeft :
- Acta crystallogr, Assay, Bcov aibv, Biol, Biol chem, Biology organization, Cellular organisms, Cellular primases, Coronavirus, Coronaviruses, Crystal structure, Dengue virus, Dgtp, Embo, Embo journal, Essential residues, Eukaryotic primases, Genome, Gorbalenya, Human coronavirus, Imbert, Ns5b, Nsp7, Nsp8, Nsp8 activity, Nsp8 protein, Nsp8 rdrp, Nsp8 rdrp activity, Nucleic acids, Nucleotide, Nucleotide incorporation, Oligo, Polymerase, Primase, Primases, Primer, Product formation, Rdrp, Rdrp activity, Rdrps, Replicase, Replication, Rna, Sars, Sars coronavirus, Snijder, Ssrna, Ssrna template, Supplementary figure, Template, Tgev pedv, Thiel, Time course, Torovirus, Transcription, Viral, Virol, Zhai, Ziebuhr.
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.
Url:
DOI: 10.1038/sj.emboj.7601368
Affiliations:
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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><affiliations><list><country><li>France</li><li>Pays-Bas</li></country><region><li>Hollande-Méridionale</li></region><settlement><li>Leyde</li></settlement></list><tree><country name="France"><noRegion><name sortKey="Imbert, Isabelle" sort="Imbert, Isabelle" uniqKey="Imbert I" first="Isabelle" last="Imbert">Isabelle Imbert</name></noRegion><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="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="Guillemot, Jean Laude" sort="Guillemot, Jean Laude" uniqKey="Guillemot J" first="Jean-Claude" last="Guillemot">Jean-Claude Guillemot</name></country><country name="Pays-Bas"><region name="Hollande-Méridionale"><name sortKey="Gorbalenya, Alexander E" sort="Gorbalenya, Alexander E" uniqKey="Gorbalenya A" first="Alexander E" last="Gorbalenya">Alexander E. Gorbalenya</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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