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J. Biochem, 2003, Vol. 134, No. 4 505-511
© 2003 Japanese Biochemical Society

BIOCHEMISTRY

Characterization of ATPase Activity of a Hepatitis C Virus NS3 Helicase Domain, and Analysis Involving Mercuric Reagents

Kiyoshi Kyono*,1, Masahiko Miyashiro2 and Ikuhiko Taguchi2

1 Medicinal Chemistry Research Laboratories and 2 Discovery & Pharmacology Research Laboratories, Tanabe Seiyaku Co., Ltd., 16-89 Kashima 3-chome, Yodogawa-ku, Osaka 532-8505

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 Mg2+ 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.

* To whom correspondence should be addressed. Tel: +81-6-300-2574, Fax: +81-6-300-2593, E-mail: k-kyono{at}tanabe.co.jp


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