SrasV1, Main, Exploration, bibRecord, 001975

Characterization of the guanine-N7 methyltransferase activity of coronavirus nsp14 on nucleotide GTP.

Identifieur interne : 001975 ( Main/Exploration ); précédent : 001974; suivant : 001976

Characterization of the guanine-N7 methyltransferase activity of coronavirus nsp14 on nucleotide GTP.

Auteurs : Xu Jin [République populaire de Chine] ; Yu Chen ; Ying Sun ; Cong Zeng ; Yi Wang ; Jiali Tao ; Andong Wu ; Xiao Yu ; Zhou Zhang ; Jie Tian ; Deyin Guo

Source :

Virus research [ 1872-7492 ] ; 2013.

RBID : pubmed:23702198

Descripteurs français

KwdFr :
- Analyse de mutations d'ADN, Exoribonucleases (métabolisme), Guanosine triphosphate (métabolisme), Methyltransferases (métabolisme), Protéines virales non structurales (métabolisme), Spécificité du substrat.
MESH :
- métabolisme : Exoribonucleases, Guanosine triphosphate, Methyltransferases, Protéines virales non structurales.
- Analyse de mutations d'ADN, Spécificité du substrat.

English descriptors

KwdEn :
- DNA Mutational Analysis, Exoribonucleases (metabolism), Guanosine Triphosphate (metabolism), Methyltransferases (metabolism), Substrate Specificity, Viral Nonstructural Proteins (metabolism).
MESH :
- chemical , metabolism : Exoribonucleases, Guanosine Triphosphate, Methyltransferases, Viral Nonstructural Proteins.
- DNA Mutational Analysis, Substrate Specificity.

Abstract

Most eukaryotic viruses that replicate in the cytoplasm, including coronaviruses, have evolved strategies to cap their RNAs. In our previous work, the nonstructural protein (nsp) 14 of severe acute respiratory syndrome coronavirus (SARS-CoV) was identified as a cap (guanine-N7)-methyltransferase (N7-MTase). In this study, we found that GTP, dGTP as well as cap analogs GpppG, GpppA and m7GpppG could be methylated by SARS-CoV nsp14. In contrast, the nsp14 could not modify ATP, CTP, UTP, dATP, dCTP, dUTP or cap analog m7GpppA. Critical residues of nsp14 essential for the methyltransferase activity on GTP were identified, which include F73, R84, W86, R310, D331, G333, P335, Y368, C414, and C416. We further showed that the methyltransferase activity of GTP was universal for nsp14 of other coronaviruses. Moreover, the accumulation of m7GTP or presence of protein nsp14 could interfere with protein translation of cellular mRNAs. Altogether, the results revealed a new enzymatic activity of coronavirus nsp14.

DOI: 10.1016/j.virusres.2013.05.001
PubMed: 23702198

Affiliations:

Le document en format XML

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<front><div type="abstract" xml:lang="en">Most eukaryotic viruses that replicate in the cytoplasm, including coronaviruses, have evolved strategies to cap their RNAs. In our previous work, the nonstructural protein (nsp) 14 of severe acute respiratory syndrome coronavirus (SARS-CoV) was identified as a cap (guanine-N7)-methyltransferase (N7-MTase). In this study, we found that GTP, dGTP as well as cap analogs GpppG, GpppA and m7GpppG could be methylated by SARS-CoV nsp14. In contrast, the nsp14 could not modify ATP, CTP, UTP, dATP, dCTP, dUTP or cap analog m7GpppA. Critical residues of nsp14 essential for the methyltransferase activity on GTP were identified, which include F73, R84, W86, R310, D331, G333, P335, Y368, C414, and C416. We further showed that the methyltransferase activity of GTP was universal for nsp14 of other coronaviruses. Moreover, the accumulation of m7GTP or presence of protein nsp14 could interfere with protein translation of cellular mRNAs. Altogether, the results revealed a new enzymatic activity of coronavirus nsp14.</div>
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Characterization of the guanine-N7 methyltransferase activity of coronavirus nsp14 on nucleotide GTP.

Characterization of the guanine-N7 methyltransferase activity of coronavirus nsp14 on nucleotide GTP.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki

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