SrasV1, Ncbi, Curation, bibRecord, 000806

Multiple Enzymatic Activities Associated with Severe Acute Respiratory Syndrome Coronavirus Helicase

Identifieur interne : 000806 ( Ncbi/Curation ); précédent : 000805; suivant : 000807

Multiple Enzymatic Activities Associated with Severe Acute Respiratory Syndrome Coronavirus Helicase

Auteurs : Konstantin A. Ivanov ; Volker Thiel ; Jessika C. Dobbe ; Yvonne Van Der Meer ; Eric J. Snijder ; John Ziebuhr

Source :

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

RBID : PMC:415832

Descripteurs français

KwdFr :
- Acid anhydride hydrolases (métabolisme), Animaux, Cellules Vero, Données de séquences moléculaires, Helicase (métabolisme), RNA helicases (métabolisme), Réplication virale, Séquence d'acides aminés, Virus du SRAS (enzymologie).
MESH :
- enzymologie : Virus du SRAS.
- métabolisme : Acid anhydride hydrolases, Helicase, RNA helicases.
- Animaux, Cellules Vero, Données de séquences moléculaires, Réplication virale, Séquence d'acides aminés.

English descriptors

KwdEn :
- Acid Anhydride Hydrolases (metabolism), Amino Acid Sequence, Animals, Chlorocebus aethiops, DNA Helicases (metabolism), Molecular Sequence Data, RNA Helicases (metabolism), SARS Virus (enzymology), Vero Cells, Virus Replication.
MESH :
- chemical , metabolism : Acid Anhydride Hydrolases, DNA Helicases, RNA Helicases.
- enzymology : SARS Virus.
- Amino Acid Sequence, Animals, Chlorocebus aethiops, Molecular Sequence Data, Vero Cells, Virus Replication.

Abstract

Severe acute respiratory syndrome coronavirus (SARS-CoV), a newly identified group 2 coronavirus, is the causative agent of severe acute respiratory syndrome, a life-threatening form of pneumonia in humans. Coronavirus replication and transcription are highly specialized processes of cytoplasmic RNA synthesis that localize to virus-induced membrane structures and were recently proposed to involve a complex enzymatic machinery that, besides RNA-dependent RNA polymerase, helicase, and protease activities, also involves a series of RNA-processing enzymes that are not found in most other RNA virus families. Here, we characterized the enzymatic activities of a recombinant form of the SARS-CoV helicase (nonstructural protein [nsp] 13), a superfamily 1 helicase with an N-terminal zinc-binding domain. We report that nsp13 has both RNA and DNA duplex-unwinding activities. SARS-CoV nsp13 unwinds its substrates in a 5′-to-3′ direction and features a remarkable processivity, allowing efficient strand separation of extended regions of double-stranded RNA and DNA. Characterization of the nsp13-associated (deoxy)nucleoside triphosphatase ([dNTPase) activities revealed that all natural nucleotides and deoxynucleotides are substrates of nsp13, with ATP, dATP, and GTP being hydrolyzed slightly more efficiently than other nucleotides. Furthermore, we established an RNA 5′-triphosphatase activity for the SARS-CoV nsp13 helicase which may be involved in the formation of the 5′ cap structure of viral RNAs. The data suggest that the (d)NTPase and RNA 5′-triphosphatase activities of nsp13 have a common active site. Finally, we established that, in SARS-CoV-infected Vero E6 cells, nsp13 localizes to membranes that appear to be derived from the endoplasmic reticulum and are the likely site of SARS-CoV RNA synthesis.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC415832

DOI: 10.1128/JVI.78.11.5619-5632.2004
PubMed: 15140959
PubMed Central: 415832

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PMC:415832

Le document en format XML

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<term>Données de séquences moléculaires</term>
<term>Helicase (métabolisme)</term>
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<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en"><p>Severe acute respiratory syndrome coronavirus (SARS-CoV), a newly identified group 2 coronavirus, is the causative agent of severe acute respiratory syndrome, a life-threatening form of pneumonia in humans. Coronavirus replication and transcription are highly specialized processes of cytoplasmic RNA synthesis that localize to virus-induced membrane structures and were recently proposed to involve a complex enzymatic machinery that, besides RNA-dependent RNA polymerase, helicase, and protease activities, also involves a series of RNA-processing enzymes that are not found in most other RNA virus families. Here, we characterized the enzymatic activities of a recombinant form of the SARS-CoV helicase (nonstructural protein [nsp] 13), a superfamily 1 helicase with an N-terminal zinc-binding domain. We report that nsp13 has both RNA and DNA duplex-unwinding activities. SARS-CoV nsp13 unwinds its substrates in a 5′-to-3′ direction and features a remarkable processivity, allowing efficient strand separation of extended regions of double-stranded RNA and DNA. Characterization of the nsp13-associated (deoxy)nucleoside triphosphatase ([dNTPase) activities revealed that all natural nucleotides and deoxynucleotides are substrates of nsp13, with ATP, dATP, and GTP being hydrolyzed slightly more efficiently than other nucleotides. Furthermore, we established an RNA 5′-triphosphatase activity for the SARS-CoV nsp13 helicase which may be involved in the formation of the 5′ cap structure of viral RNAs. The data suggest that the (d)NTPase and RNA 5′-triphosphatase activities of nsp13 have a common active site. Finally, we established that, in SARS-CoV-infected Vero E6 cells, nsp13 localizes to membranes that appear to be derived from the endoplasmic reticulum and are the likely site of SARS-CoV RNA synthesis.</p>
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Multiple Enzymatic Activities Associated with Severe Acute Respiratory Syndrome Coronavirus Helicase

Multiple Enzymatic Activities Associated with Severe Acute Respiratory Syndrome Coronavirus Helicase

Source :

Descripteurs français

English descriptors

Abstract

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

Links to Exploration step

Le document en format XML

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Pour générer des pages wiki