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Hepatitis C virus NS3 RNA helicase activity is modulated by the two domains of NS3 and NS4A.

Abstract：

:To determine whether the two domains of hepatitis C virus (HCV) NS3 and the NS4A interact with each other to regulate the RNA unwinding activity, this study compares the RNA unwinding, ATPase and RNA binding activities of three forms of NS3 proteins--the NS3H protein, containing only the helicase domain, the full-length NS3 protein, and the NS3-NS4A complex. The results revealed that NS3 displayed the weakest RNA helicase activity, not because it had lower ATPase or RNA binding activity than did NS3H or NS3-NS4A, but because it had the lowest RNA unwinding processivity. A mutant protein, R1487Q, which contained a mutation in the helicase domain, displayed a reduced protease activity as compared to the wild-type NS3-NS4A. Together, these results suggest the existence of interactions between the two domains of NS3 and the NS4A, which regulates the HCV NS3 protease and RNA helicase activities.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kuang WF,Lin YC,Jean F,Huang YW,Tai CL,Chen DS,Chen PJ,Hwang LH

doi

10.1016/j.bbrc.2004.03.032

subject

Has Abstract

pub_date

2004-04-23 00:00:00

pages

211-7

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006291X04005108

journal_volume

317

pub_type

杂志文章

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