SrasV1, Main, Merge, bibRecord, 005392

The Severe Acute Respiratory Syndrome Coronavirus Nsp15 Protein Is an Endoribonuclease That Prefers Manganese as a Cofactor

Identifieur interne : 005392 ( Main/Merge ); précédent : 005391; suivant : 005393

The Severe Acute Respiratory Syndrome Coronavirus Nsp15 Protein Is an Endoribonuclease That Prefers Manganese as a Cofactor

Auteurs : Kanchan Bhardwaj [États-Unis] ; Linda Guarino [États-Unis] ; C. Cheng Kao [États-Unis]

Source :

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

RBID : PMC:525082

Descripteurs français

KwdFr :
- Données de séquences moléculaires, Endoribonucleases (métabolisme), Manganèse (pharmacologie), Protéines virales non structurales (), Protéines virales non structurales (métabolisme), Séquence d'acides aminés, Virus du SRAS (enzymologie).
MESH :
- enzymologie : Virus du SRAS.
- métabolisme : Endoribonucleases, Protéines virales non structurales.
- pharmacologie : Manganèse.
- Données de séquences moléculaires, Protéines virales non structurales, Séquence d'acides aminés.

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. Mn²⁺ at 2 to 10 mM was needed for optimal endoribonuclease activity, but Mg²⁺ and several other divalent metals were capable of supporting only a low level of activity. Concentrations of Mn²⁺ 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.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC525082

DOI: 10.1128/JVI.78.22.12218-12224.2004
PubMed: 15507608
PubMed Central: 525082

Links to Exploration step

PMC:525082

Le document en format XML

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<front><div type="abstract" xml:lang="en"><p>Nonstructural protein 15 (Nsp15) of the severe acute respiratory syndrome coronavirus (SARS-CoV) produced in <italic>Escherichia coli</italic>
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 and several other divalent metals were capable of supporting only a low level of activity. Concentrations of Mn<sup>2+</sup>
 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.</p>
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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 :

Descripteurs français

English descriptors

Abstract

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

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

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