SrasV1, PubMed, Corpus, bibRecord, 002092

Coronavirus nucleocapsid protein is an RNA chaperone.

Identifieur interne : 002092 ( PubMed/Corpus ); précédent : 002091; suivant : 002093

Coronavirus nucleocapsid protein is an RNA chaperone.

Auteurs : Sonia Zú Iga ; Isabel Sola ; Jose L. Moreno ; Patricia Sabella ; Juan Plana-Durán ; Luis Enjuanes

Source :

Virology [ 0042-6822 ] ; 2007.

RBID : pubmed:16979208

English descriptors

KwdEn :
- Chaperonins (chemistry), Chaperonins (metabolism), Coronavirus (chemistry), Genome, Viral (physiology), Molecular Chaperones (chemistry), Molecular Chaperones (metabolism), Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (genetics), Nucleocapsid Proteins (metabolism), RNA, Catalytic (chemistry), RNA, Catalytic (genetics), RNA, Catalytic (metabolism), RNA, Viral (metabolism), Virus Replication (physiology).
MESH :
- chemical , chemistry : Chaperonins, Molecular Chaperones, Nucleocapsid Proteins, RNA, Catalytic.
- chemical , genetics : Nucleocapsid Proteins, RNA, Catalytic.
- chemical , metabolism : Chaperonins, Molecular Chaperones, Nucleocapsid Proteins, RNA, Catalytic, RNA, Viral.
- chemistry : Coronavirus.
- physiology : Genome, Viral, Virus Replication.

Abstract

RNA chaperones are nonspecific nucleic acid binding proteins with long disordered regions that help RNA molecules to adopt its functional conformation. Coronavirus nucleoproteins (N) are nonspecific RNA-binding proteins with long disordered regions. Therefore, we investigated whether transmissible gastroenteritis coronavirus (TGEV) N protein was an RNA chaperone. Purified N protein enhanced hammerhead ribozyme self-cleavage and nucleic acids annealing, which are properties that define RNA chaperones. In contrast, another RNA-binding protein, PTB, did not show these activities. N protein chaperone activity was blocked by specific monoclonal antibodies. Therefore, it was concluded that TGEV N protein is an RNA chaperone. In addition, we have shown that purified severe acute respiratory syndrome (SARS)-CoV N protein also has RNA chaperone activity. In silico predictions of disordered domains showed a similar pattern for all coronavirus N proteins evaluated. Altogether, these data led us to suggest that all coronavirus N proteins might be RNA chaperones.

DOI: 10.1016/j.virol.2006.07.046
PubMed: 16979208

Links to Exploration step

pubmed:16979208

Le document en format XML

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<front><div type="abstract" xml:lang="en">RNA chaperones are nonspecific nucleic acid binding proteins with long disordered regions that help RNA molecules to adopt its functional conformation. Coronavirus nucleoproteins (N) are nonspecific RNA-binding proteins with long disordered regions. Therefore, we investigated whether transmissible gastroenteritis coronavirus (TGEV) N protein was an RNA chaperone. Purified N protein enhanced hammerhead ribozyme self-cleavage and nucleic acids annealing, which are properties that define RNA chaperones. In contrast, another RNA-binding protein, PTB, did not show these activities. N protein chaperone activity was blocked by specific monoclonal antibodies. Therefore, it was concluded that TGEV N protein is an RNA chaperone. In addition, we have shown that purified severe acute respiratory syndrome (SARS)-CoV N protein also has RNA chaperone activity. In silico predictions of disordered domains showed a similar pattern for all coronavirus N proteins evaluated. Altogether, these data led us to suggest that all coronavirus N proteins might be RNA chaperones.</div>
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<Abstract><AbstractText>RNA chaperones are nonspecific nucleic acid binding proteins with long disordered regions that help RNA molecules to adopt its functional conformation. Coronavirus nucleoproteins (N) are nonspecific RNA-binding proteins with long disordered regions. Therefore, we investigated whether transmissible gastroenteritis coronavirus (TGEV) N protein was an RNA chaperone. Purified N protein enhanced hammerhead ribozyme self-cleavage and nucleic acids annealing, which are properties that define RNA chaperones. In contrast, another RNA-binding protein, PTB, did not show these activities. N protein chaperone activity was blocked by specific monoclonal antibodies. Therefore, it was concluded that TGEV N protein is an RNA chaperone. In addition, we have shown that purified severe acute respiratory syndrome (SARS)-CoV N protein also has RNA chaperone activity. In silico predictions of disordered domains showed a similar pattern for all coronavirus N proteins evaluated. Altogether, these data led us to suggest that all coronavirus N proteins might be RNA chaperones.</AbstractText>
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Coronavirus nucleocapsid protein is an RNA chaperone.

Coronavirus nucleocapsid protein is an RNA chaperone.

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