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J Gen Virol 86 (2005), 521-526; DOI 10.1099/vir.0.80492-0

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© 2005 Society for General Microbiology

Short Communication

Back-priming mode of {phi}6 RNA-dependent RNA polymerase

Minni R. L. Laurila1,{dagger}, Paula S. Salgado2,{dagger}, David I. Stuart2, Jonathan M. Grimes2 and Dennis H. Bamford1

1 Institute of Biotechnology and Department of Biological and Environmental Sciences, Viikki Biocenter, PO Box 56 (Viikinkaari 5), 00014 University of Helsinki, Finland
2 Division of Structural Biology, The Henry Wellcome Building for Genomic Medicine, Oxford University, Roosevelt Drive, Oxford OX3 7BN, UK

Correspondence
Dennis H. Bamford
dennis.bamford{at}helsinki.fi

The RNA-dependent RNA polymerase of the double-stranded RNA bacteriophage {phi}6 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.

{dagger}These authors contributed equally to the work.

The coordinates and structure factors of the SG mutant model have been deposited in the Protein Database with accession codes 1WAC and R1WAC, respectively.

Information on data collection and refinement statistics is available as supplementary material in JGV Online.




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