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The C-terminal priming domain is strongly associated with the main body of bacteriophage phi 6 RNA-dependent RNA polymerase

DOI: 10.1016/j.virol.2012.05.035 DOI Help

Authors: L. Peter Sarin (University of Helsinki, Finland) , Sam Wright (Oxford University, U.K.) , Qing Chen (University of Helsinki, Finland) , Linda H. Degerth (University of Helsinki, Finland) , David I. Stuart (Diamond Light Source) , Jonathan M. Grimes (Division of Structural Biology, University of Oxford) , Dennis H. Bamford (University of Helsinki, Finland) , Minna M. Poranen (University of Helsinki, Finland)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Virology , VOL 432 (1) , PAGES 184-193

State: Published (Approved)
Published: October 2012

Abstract: Double-stranded RNA viruses encode a single protein species containing RNA-dependent RNA polymerase (RdRP) motifs. This protein is responsible for RNA transcription and replication. The architecture of viral RdRPs resembles that of a cupped right hand with fingers, palm and thumb domains. Those using de novo initiation have a flexible structural elaboration that constitutes the priming platform. Here we investigate the properties of the C-terminal priming domain of bacteriophage phi 6 to get insights into the role of an extended loop connecting this domain to the main body of the polymerase. Proteolyzed phi 6 RdRP that possesses a nick in the hinge region of this loop was better suited for de novo initiation. The clipped C-terminus remained associated with the main body of the polymerase via the anchor helix. The structurally flexible hinge region appeared to be involved in the control of priming platform movement. Moreover, we detected abortive initiation products for a bacteriophage RdRP. (C) 2012 Elsevier Inc. All rights reserved.

Journal Keywords: Rna-Dependent Rna Polymerase; Priming Domain; Viral Genome Replication; Bacteriophage Phi 6; Dsrna Virus

Subject Areas: Biology and Bio-materials


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Added On: 08/10/2012 14:25

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