RNA 3'-end mismatch excision by the severe acute respiratory syndrome coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complex.
Identifieur interne : 000174 ( France/Analysis ); précédent : 000173; suivant : 000175RNA 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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