Multiple interactions within the hepatitis C virus RNA polymerase repress primer-dependent RNA synthesis

J Mol Biol. 2003 Jul 18;330(4):675-85. doi: 10.1016/s0022-2836(03)00613-2.

Abstract

The hepatitis C virus (HCV) RNA-dependent RNA polymerase (RdRp) initiates RNA synthesis in vivo by a de novo mechanism. In vitro, however, the HCV RdRp can initiate de novo or extend from a primed template. A novel beta-loop near the RdRp active site was previously found to prevent the use of primed templates. We found that, in addition to the beta-loop, the C-terminal tail of the HCV RdRp and the de novo initiation GTP are required to exclude the use of primed-templates. GTP binding to the NTPi site of the HCV RdRp orchestrates the participation of other structures. The interactions of the beta-loop, C-terminal tail, and GTP provide an elegant solution to ensure de novo initiation of HCV RNA synthesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • DNA-Directed RNA Polymerases / metabolism*
  • Dose-Response Relationship, Drug
  • Escherichia coli / metabolism
  • Guanosine Triphosphate / metabolism
  • Hepacivirus / enzymology*
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Nucleic Acid Conformation
  • Protein Structure, Tertiary
  • RNA / biosynthesis*
  • RNA, Viral*
  • Viral Nonstructural Proteins / chemistry

Substances

  • RNA, Viral
  • Viral Nonstructural Proteins
  • RNA
  • Guanosine Triphosphate
  • NS-5 protein, hepatitis C virus
  • DNA-Directed RNA Polymerases