SrasV1, PubMed, Corpus, bibRecord, 002A78

The severe acute respiratory syndrome coronavirus Nsp15 protein is an endoribonuclease that prefers manganese as a cofactor.

Identifieur interne : 002A78 ( PubMed/Corpus ); précédent : 002A77; suivant : 002A79

The severe acute respiratory syndrome coronavirus Nsp15 protein is an endoribonuclease that prefers manganese as a cofactor.

Auteurs : Kanchan Bhardwaj ; Linda Guarino ; C Cheng Kao

Source :

Journal of virology [ 0022-538X ] ; 2004.

RBID : pubmed:15507608

English descriptors

KwdEn :
- Amino Acid Sequence, Endoribonucleases (metabolism), Manganese (pharmacology), Molecular Sequence Data, SARS Virus (enzymology), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (metabolism).
MESH :
- chemical , chemistry : Viral Nonstructural Proteins.
- chemical , metabolism : Endoribonucleases, Viral Nonstructural Proteins.
- chemical , pharmacology : Manganese.
- enzymology : SARS Virus.
- Amino Acid Sequence, Molecular Sequence Data.

Abstract

Nonstructural protein 15 (Nsp15) of the severe acute respiratory syndrome coronavirus (SARS-CoV) produced in Escherichia coli has endoribonuclease activity that preferentially cleaved 5' of uridylates of RNAs. Blocking either the 5' or 3' terminus did not affect cleavage. Double- and single-stranded RNAs were both substrates for Nsp15 but with different kinetics for cleavage. Mn(2+) at 2 to 10 mM was needed for optimal endoribonuclease activity, but Mg(2+) and several other divalent metals were capable of supporting only a low level of activity. Concentrations of Mn(2+) needed for endoribonuclease activity induced significant conformation change(s) in the protein, as measured by changes in tryptophan fluorescence. A similar endoribonucleolytic activity was detected for the orthologous protein from another coronavirus, demonstrating that the endoribonuclease activity of Nsp15 may be common to coronaviruses. This work presents an initial biochemical characterization of a novel coronavirus endoribonuclease.

DOI: 10.1128/JVI.78.22.12218-12224.2004
PubMed: 15507608

Links to Exploration step

pubmed:15507608

Le document en format XML

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<author><name sortKey="Bhardwaj, Kanchan" sort="Bhardwaj, Kanchan" uniqKey="Bhardwaj K" first="Kanchan" last="Bhardwaj">Kanchan Bhardwaj</name>
<affiliation><nlm:affiliation>Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-2128, USA.</nlm:affiliation>
</affiliation>
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<author><name sortKey="Guarino, Linda" sort="Guarino, Linda" uniqKey="Guarino L" first="Linda" last="Guarino">Linda Guarino</name>
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<author><name sortKey="Kao, C Cheng" sort="Kao, C Cheng" uniqKey="Kao C" first="C Cheng" last="Kao">C Cheng Kao</name>
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<affiliation><nlm:affiliation>Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-2128, USA.</nlm:affiliation>
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<author><name sortKey="Guarino, Linda" sort="Guarino, Linda" uniqKey="Guarino L" first="Linda" last="Guarino">Linda Guarino</name>
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<term>Molecular Sequence Data</term>
<term>SARS Virus (enzymology)</term>
<term>Viral Nonstructural Proteins (chemistry)</term>
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<front><div type="abstract" xml:lang="en">Nonstructural protein 15 (Nsp15) of the severe acute respiratory syndrome coronavirus (SARS-CoV) produced in Escherichia coli has endoribonuclease activity that preferentially cleaved 5' of uridylates of RNAs. Blocking either the 5' or 3' terminus did not affect cleavage. Double- and single-stranded RNAs were both substrates for Nsp15 but with different kinetics for cleavage. Mn(2+) at 2 to 10 mM was needed for optimal endoribonuclease activity, but Mg(2+) and several other divalent metals were capable of supporting only a low level of activity. Concentrations of Mn(2+) needed for endoribonuclease activity induced significant conformation change(s) in the protein, as measured by changes in tryptophan fluorescence. A similar endoribonucleolytic activity was detected for the orthologous protein from another coronavirus, demonstrating that the endoribonuclease activity of Nsp15 may be common to coronaviruses. This work presents an initial biochemical characterization of a novel coronavirus endoribonuclease.</div>
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<Abstract><AbstractText>Nonstructural protein 15 (Nsp15) of the severe acute respiratory syndrome coronavirus (SARS-CoV) produced in Escherichia coli has endoribonuclease activity that preferentially cleaved 5' of uridylates of RNAs. Blocking either the 5' or 3' terminus did not affect cleavage. Double- and single-stranded RNAs were both substrates for Nsp15 but with different kinetics for cleavage. Mn(2+) at 2 to 10 mM was needed for optimal endoribonuclease activity, but Mg(2+) and several other divalent metals were capable of supporting only a low level of activity. Concentrations of Mn(2+) needed for endoribonuclease activity induced significant conformation change(s) in the protein, as measured by changes in tryptophan fluorescence. A similar endoribonucleolytic activity was detected for the orthologous protein from another coronavirus, demonstrating that the endoribonuclease activity of Nsp15 may be common to coronaviruses. This work presents an initial biochemical characterization of a novel coronavirus endoribonuclease.</AbstractText>
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The severe acute respiratory syndrome coronavirus Nsp15 protein is an endoribonuclease that prefers manganese as a cofactor.

The severe acute respiratory syndrome coronavirus Nsp15 protein is an endoribonuclease that prefers manganese as a cofactor.

Source :

English descriptors

Abstract

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

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