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The RNA-dependent RNA polymerase of the double-stranded RNA bacteriophage phi6 is capable of primer-independent initiation, as are many RNA polymerases. The structure of this polymerase revealed an initiation platform, composed of a loop in the C-terminal domain (QYKW, aa 629-632), that was essential for de novo initiation. A similar element has been identified in hepatitis C virus RNA-dependent RNA polymerase. Biochemical studies have addressed the role of this platform, revealing that a mutant version can utilize a back-priming initiation mechanism, where the 3' terminus of the template adopts a hairpin-like conformation. Here, the mechanism of back-primed initiation is studied further by biochemical and structural methods.

Original publication

DOI

10.1099/vir.0.80492-0

Type

Journal article

Journal

J Gen Virol

Publication Date

02/2005

Volume

86

Pages

521 - 526

Keywords

Bacteriophage phi 6, Base Sequence, Models, Molecular, Molecular Sequence Data, Mutation, Nucleic Acid Conformation, Pseudomonas, RNA Replicase, RNA, Viral, Templates, Genetic