HCV NS3 protein helicase domain assists RNA structure conversion.
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.
Huang
Zhi-Shun
ZS
Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
Wang
Chun-Chung
CC
Wu
Huey-Nan
HN
D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D020816:Amino Acid Motifs / Q000235:genetics; D004265:DNA Helicases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D016174:Hepacivirus / Q000235:genetics / Q000378:metabolism*; D006868:Hydrolysis; D017434:Protein Structure, Tertiary / Q000235:genetics; D012313:RNA / Q000235:genetics / Q000378:metabolism*; D012330:RNA, Double-Stranded / Q000235:genetics / Q000378:metabolism*
D012330:RNA, Double-Stranded; D012313:RNA; D000251:Adenosine Triphosphatases; D004265:DNA Helicases