Characterization of ATPase activity of a hepatitis C virus NS3 helicase domain, and analysis involving mercuric reagents.

Characterization of ATPase activity of a hepatitis C virus NS3 helicase domain, and analysis involving mercuric reagents. Research Abstract Details 

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Characterization of ATPase activity of a hepatitis C virus NS3 helicase domain, and analysis involving mercuric reagents. Abstract Text:

Kiyoshi Kyono,Masahiko Miyashiro,Ikuhiko Taguchi,

The C-terminal two-thirds of nonstructural protein 3 (NS3) of hepatitis C virus (HCV) exhibits RNA-dependent NTPase/helicase activity. This enzyme is considered to be involved in viral replication and is expected to be one of the target molecules of anti-HCV drugs. In a search for NTPase inhibitors specific to HCV, we expressed and purified the truncated NS3 NTPase/helicase domain. Here, we report the characterization of its RNA-dependent ATPase activity. This enzyme preferred Mg(2+) and the optimal pH was 7.0. We further investigated the effects of heavy metal ions on the ATPase activity. The mercuric ion inhibited it significantly, the 50% inhibitory concentration being 49 nM. The fact that the inhibitory profile was competitive and that this inhibition was blocked in the presence of a large excess of cysteine or dithiothreitol, suggested that a cysteine residue in the DECH box was the main target site of mercury.

Characterization of ATPase activity of a hepatitis C virus NS3 helicase domain, and analysis involving mercuric reagents. Publishing Authors By Initials

K Kyono,M Miyashiro,I Taguchi,

For similar proteins: viral proteins: viral nonstructural proteins research abstracts see: proteins: viral proteins: viral nonstructural proteins research

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Characterization of ATPase activity of a hepatitis C virus NS3 helicase domain, and analysis involving mercuric reagents. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 134

Page Numbers: 505-11

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Oct

YEAR: 2003

Characterization of ATPase activity of a hepatitis C virus NS3 helicase domain, and analysis involving mercuric reagents. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Characterization of ATPase activity of a hepatitis C virus NS3 helicase domain, and analysis involving mercuric reagents. Keywords Mesh Terms:

KEYWORDS: Viral Nonstructural Proteins

MESH TERMS: chemistry

Chemical & Substance for Abstract: Characterization of ATPase activity of a hepatitis C virus NS3 helicase domain, and analysis involving mercuric reagents. Information

Substance Name: Adenosine Triphosphatases

Registry Number: EC 3.6.1.-

Grant and Affiliation Information for Characterization of ATPase activity of a hepatitis C virus NS3 helicase domain, and analysis involving mercuric reagents.

AFFILIATION: Medicinal Chemistry Research Laboratories, Tanabe Seiyaku Co., Ltd., 16-89 Kashima 3-chome, Yodogawa-ku, Osaka 532-8505. k-kyono@tanabe.co.jp

Country: Japan

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MEDLINETA: J Biochem

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