RNA 3'-end mismatch excision by the severe acute respiratory syndrome coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complex.
Identifieur interne : 001309 ( PubMed/Checkpoint ); précédent : 001308; suivant : 001310RNA 3'-end mismatch excision by the severe acute respiratory syndrome coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complex.
Auteurs : Mickaël Bouvet [France] ; Isabelle Imbert ; Lorenzo Subissi ; Laure Gluais ; Bruno Canard ; Etienne DecrolySource :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2012.
Descripteurs français
- KwdFr :
- ARN viral (génétique), Cadres ouverts de lecture, Exoribonucleases (génétique), Exoribonucleases (métabolisme), Maturation post-transcriptionnelle des ARN, Mésappariement de bases, Protéines virales non structurales (génétique), Protéines virales non structurales (métabolisme), Virus du SRAS (génétique).
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Exoribonucleases, RNA, Viral, Viral Nonstructural Proteins.
- chemical , metabolism : Exoribonucleases, Viral Nonstructural Proteins.
- genetics : SARS Virus.
- Base Pair Mismatch, Open Reading Frames, RNA Processing, Post-Transcriptional.
Abstract
The replication/transcription complex of severe acute respiratory syndrome coronavirus is composed of at least 16 nonstructural proteins (nsp1-16) encoded by the ORF-1a/1b. This complex includes replication enzymes commonly found in positive-strand RNA viruses, but also a set of RNA-processing activities unique to some nidoviruses. The nsp14 protein carries both exoribonuclease (ExoN) and (guanine-N7)-methyltransferase (N7-MTase) activities. The nsp14 ExoN activity ensures a yet-uncharacterized function in the virus life cycle and must be regulated to avoid nonspecific RNA degradation. In this work, we show that the association of nsp10 with nsp14 stimulates >35-fold the ExoN activity of the latter while playing no effect on N7-MTase activity. Nsp10 mutants unable to interact with nsp14 are not proficient for ExoN activation. The nsp10/nsp14 complex hydrolyzes double-stranded RNA in a 3' to 5' direction as well as a single mismatched nucleotide at the 3'-end mimicking an erroneous replication product. In contrast, di-, tri-, and longer unpaired ribonucleotide stretches, as well as 3'-modified RNAs, resist nsp10/nsp14-mediated excision. In addition to the activation of nsp16-mediated 2'-O-MTase activity, nsp10 also activates nsp14 in an RNA processing function potentially connected to a replicative mismatch repair mechanism.
DOI: 10.1073/pnas.1201130109
PubMed: 22635272
Affiliations:
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pubmed:22635272Le document en format XML
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xml:lang="fr"><term>ARN viral</term><term>Exoribonucleases</term><term>Protéines virales non structurales</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Exoribonucleases</term><term>Protéines virales non structurales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Base Pair Mismatch</term><term>Open Reading Frames</term><term>RNA Processing, Post-Transcriptional</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cadres ouverts de lecture</term><term>Maturation post-transcriptionnelle des ARN</term><term>Mésappariement de bases</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The replication/transcription complex of severe acute respiratory syndrome coronavirus is composed of at least 16 nonstructural proteins (nsp1-16) encoded by the ORF-1a/1b. This complex includes replication enzymes commonly found in positive-strand RNA viruses, but also a set of RNA-processing activities unique to some nidoviruses. The nsp14 protein carries both exoribonuclease (ExoN) and (guanine-N7)-methyltransferase (N7-MTase) activities. The nsp14 ExoN activity ensures a yet-uncharacterized function in the virus life cycle and must be regulated to avoid nonspecific RNA degradation. In this work, we show that the association of nsp10 with nsp14 stimulates >35-fold the ExoN activity of the latter while playing no effect on N7-MTase activity. Nsp10 mutants unable to interact with nsp14 are not proficient for ExoN activation. The nsp10/nsp14 complex hydrolyzes double-stranded RNA in a 3' to 5' direction as well as a single mismatched nucleotide at the 3'-end mimicking an erroneous replication product. In contrast, di-, tri-, and longer unpaired ribonucleotide stretches, as well as 3'-modified RNAs, resist nsp10/nsp14-mediated excision. In addition to the activation of nsp16-mediated 2'-O-MTase activity, nsp10 also activates nsp14 in an RNA processing function potentially connected to a replicative mismatch repair mechanism.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22635272</PMID><DateCompleted><Year>2012</Year><Month>08</Month><Day>28</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN><JournalIssue CitedMedium="Internet"><Volume>109</Volume><Issue>24</Issue><PubDate><Year>2012</Year><Month>Jun</Month><Day>12</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc. Natl. Acad. Sci. U.S.A.</ISOAbbreviation></Journal><ArticleTitle>RNA 3'-end mismatch excision by the severe acute respiratory syndrome coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complex.</ArticleTitle><Pagination><MedlinePgn>9372-7</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.1201130109</ELocationID><Abstract><AbstractText>The replication/transcription complex of severe acute respiratory syndrome coronavirus is composed of at least 16 nonstructural proteins (nsp1-16) encoded by the ORF-1a/1b. This complex includes replication enzymes commonly found in positive-strand RNA viruses, but also a set of RNA-processing activities unique to some nidoviruses. The nsp14 protein carries both exoribonuclease (ExoN) and (guanine-N7)-methyltransferase (N7-MTase) activities. The nsp14 ExoN activity ensures a yet-uncharacterized function in the virus life cycle and must be regulated to avoid nonspecific RNA degradation. In this work, we show that the association of nsp10 with nsp14 stimulates >35-fold the ExoN activity of the latter while playing no effect on N7-MTase activity. Nsp10 mutants unable to interact with nsp14 are not proficient for ExoN activation. The nsp10/nsp14 complex hydrolyzes double-stranded RNA in a 3' to 5' direction as well as a single mismatched nucleotide at the 3'-end mimicking an erroneous replication product. In contrast, di-, tri-, and longer unpaired ribonucleotide stretches, as well as 3'-modified RNAs, resist nsp10/nsp14-mediated excision. In addition to the activation of nsp16-mediated 2'-O-MTase activity, nsp10 also activates nsp14 in an RNA processing function potentially connected to a replicative mismatch repair mechanism.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bouvet</LastName><ForeName>Mickaël</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Architecture et Fonction des Macromolécules Biologiques, Unité Mixte de Recherche 7257, Ecole Supérieure d'Ingénieurs de Luminy Case 925, Centre National de la Recherche Scientifique and Aix-Marseille Université, 13288 Marseille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Imbert</LastName><ForeName>Isabelle</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Subissi</LastName><ForeName>Lorenzo</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Gluais</LastName><ForeName>Laure</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Canard</LastName><ForeName>Bruno</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Decroly</LastName><ForeName>Etienne</ForeName><Initials>E</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>2012</Year><Month>05</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C558878">Nsp10 protein, SARS virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012367">RNA, 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sort="Imbert, Isabelle" uniqKey="Imbert I" first="Isabelle" last="Imbert">Isabelle Imbert</name><name sortKey="Subissi, Lorenzo" sort="Subissi, Lorenzo" uniqKey="Subissi L" first="Lorenzo" last="Subissi">Lorenzo Subissi</name></noCountry><country name="France"><region name="Provence-Alpes-Côte d'Azur"><name sortKey="Bouvet, Mickael" sort="Bouvet, Mickael" uniqKey="Bouvet M" first="Mickaël" last="Bouvet">Mickaël Bouvet</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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