Biochemical characterization of a recombinant SARS coronavirus nsp12 RNA-dependent RNA polymerase capable of copying viral RNA templates.
Identifieur interne : 001338 ( PubMed/Curation ); précédent : 001337; suivant : 001339Biochemical characterization of a recombinant SARS coronavirus nsp12 RNA-dependent RNA polymerase capable of copying viral RNA templates.
Auteurs : Dae-Gyun Ahn [Corée du Sud] ; Jin-Kyu Choi ; Deborah R. Taylor ; Jong-Won OhSource :
- Archives of virology [ 1432-8798 ] ; 2012.
Descripteurs français
- KwdFr :
- ARN viral (métabolisme), Amorces ADN (génétique), Cations divalents (métabolisme), Coenzymes (métabolisme), Génome viral, Manganèse (métabolisme), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), RNA replicase (génétique), RNA replicase (métabolisme), Régions 3' non traduites, Virus du SRAS (enzymologie), Virus du SRAS (génétique).
- MESH :
- enzymologie : Virus du SRAS.
- génétique : Amorces ADN, Protéines recombinantes, RNA replicase, Virus du SRAS.
- métabolisme : ARN viral, Cations divalents, Coenzymes, Manganèse, Protéines recombinantes, RNA replicase.
- Génome viral, Régions 3' non traduites.
English descriptors
- KwdEn :
- 3' Untranslated Regions, Cations, Divalent (metabolism), Coenzymes (metabolism), DNA Primers (genetics), Genome, Viral, Manganese (metabolism), RNA Replicase (genetics), RNA Replicase (metabolism), RNA, Viral (metabolism), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), SARS Virus (enzymology), SARS Virus (genetics).
- MESH :
- chemical , genetics : DNA Primers, RNA Replicase, Recombinant Proteins.
- chemical , metabolism : Cations, Divalent, Coenzymes, Manganese, RNA Replicase, RNA, Viral, Recombinant Proteins.
- chemical : 3' Untranslated Regions.
- enzymology : SARS Virus.
- genetics : SARS Virus.
- Genome, Viral.
Abstract
The severe acute respiratory syndrome coronavirus (SARS-CoV) RNA genome is replicated by a virus-encoded RNA replicase, the key component of which is the nonstructural protein 12 (nsp12). In this report, we describe the biochemical properties of a full-length recombinant SARS-CoV nsp12 RNA-dependent RNA polymerase (RdRp) capable of copying viral RNA templates. The purified SARS-CoV nsp12 showed both primer-dependent and primer-independent RNA synthesis activities using homopolymeric RNA templates. The RdRp activity was strictly dependent on Mn(2+). The nsp12 preferentially copied homopolymeric pyrimidine RNA templates in the absence of an added oligonucleotide primer. It was also able to initiate de novo RNA synthesis from the 3'-ends of both the plus- and minus-strand genome of SARS-CoV, using the 3'-terminal 36- and 37-nt RNA, respectively. The in vitro RdRp assay system established with a full-length nsp12 will be useful for understanding the mechanisms of coronavirus replication and for the development of anti-SARS-CoV agents.
DOI: 10.1007/s00705-012-1404-x
PubMed: 22791111
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Taylor</name></author><author><name sortKey="Oh, Jong Won" sort="Oh, Jong Won" uniqKey="Oh J" first="Jong-Won" last="Oh">Jong-Won Oh</name></author></analytic><series><title level="j">Archives of virology</title><idno type="eISSN">1432-8798</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>3' Untranslated Regions</term><term>Cations, Divalent (metabolism)</term><term>Coenzymes (metabolism)</term><term>DNA Primers (genetics)</term><term>Genome, Viral</term><term>Manganese (metabolism)</term><term>RNA Replicase (genetics)</term><term>RNA Replicase (metabolism)</term><term>RNA, Viral (metabolism)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>SARS Virus (enzymology)</term><term>SARS Virus (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN viral (métabolisme)</term><term>Amorces ADN (génétique)</term><term>Cations divalents (métabolisme)</term><term>Coenzymes (métabolisme)</term><term>Génome viral</term><term>Manganèse (métabolisme)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>RNA replicase (génétique)</term><term>RNA replicase (métabolisme)</term><term>Régions 3' non traduites</term><term>Virus du SRAS (enzymologie)</term><term>Virus du SRAS (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA Primers</term><term>RNA Replicase</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cations, Divalent</term><term>Coenzymes</term><term>Manganese</term><term>RNA Replicase</term><term>RNA, Viral</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>3' Untranslated Regions</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Amorces ADN</term><term>Protéines recombinantes</term><term>RNA replicase</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN viral</term><term>Cations divalents</term><term>Coenzymes</term><term>Manganèse</term><term>Protéines recombinantes</term><term>RNA replicase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Genome, Viral</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Génome viral</term><term>Régions 3' non traduites</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome coronavirus (SARS-CoV) RNA genome is replicated by a virus-encoded RNA replicase, the key component of which is the nonstructural protein 12 (nsp12). In this report, we describe the biochemical properties of a full-length recombinant SARS-CoV nsp12 RNA-dependent RNA polymerase (RdRp) capable of copying viral RNA templates. The purified SARS-CoV nsp12 showed both primer-dependent and primer-independent RNA synthesis activities using homopolymeric RNA templates. The RdRp activity was strictly dependent on Mn(2+). The nsp12 preferentially copied homopolymeric pyrimidine RNA templates in the absence of an added oligonucleotide primer. It was also able to initiate de novo RNA synthesis from the 3'-ends of both the plus- and minus-strand genome of SARS-CoV, using the 3'-terminal 36- and 37-nt RNA, respectively. The in vitro RdRp assay system established with a full-length nsp12 will be useful for understanding the mechanisms of coronavirus replication and for the development of anti-SARS-CoV agents.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22791111</PMID><DateCompleted><Year>2013</Year><Month>01</Month><Day>15</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1432-8798</ISSN><JournalIssue CitedMedium="Internet"><Volume>157</Volume><Issue>11</Issue><PubDate><Year>2012</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Archives of virology</Title><ISOAbbreviation>Arch. 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The nsp12 preferentially copied homopolymeric pyrimidine RNA templates in the absence of an added oligonucleotide primer. It was also able to initiate de novo RNA synthesis from the 3'-ends of both the plus- and minus-strand genome of SARS-CoV, using the 3'-terminal 36- and 37-nt RNA, respectively. 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