HCV NS3 protein helicase domain assists RNA structure conversion

被引:8
作者
Huang, Zhi-Shun [1 ]
Wang, Chun-Chung [1 ,2 ]
Wu, Huey-Nan [1 ]
机构
[1] Acad Sinica, Inst Mol Biol, Taipei 115, Taiwan
[2] Natl Def Univ, Coll Med, Grad Inst Life Sci, Taipei, Taiwan
关键词
HCV NS3 helicase; RNA structure conversion; Strand annealing; dsRNA unwinding; RNA chaperone; DExH/D-box protein; ANNEALING ACTIVITIES; REARRANGEMENT;
D O I
10.1016/j.febslet.2010.04.020
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
NS3H, the helicase domain of HCV NS3, possesses RNA-stimulated ATPase and ATP hydrolysis-dependent dsRNA unwinding activities. Here, the ability of NS3H to facilitate RNA structural rearrangement is studied using relatively long RNA strands as the model substrates. NS3H promotes intermolecular annealing, resolves three-stranded RNA duplexes, and assists dsRNA and ssRNA inter-conversions to establish a steady state among RNA structures. NS3H facilitates RNA structure conversions in a mode distinct from an ATP-independent RNA chaperone. These findings expand the known function of HCV NS3 helicase and reveal a role for viral helicase in assisting RNA structure conversions during virus life cycle. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
引用
收藏
页码:2356 / 2362
页数:7
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