Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Genome replication and transcription of riboviruses are catalyzed by an RNA-dependent RNA polymerase (RdRP). RdRPs are normally associated with other virus- or/and host-encoded proteins that modulate RNA polymerization activity and template specificity. The polymerase complex of double-stranded dsRNA viruses is a large icosahedral particle (inner core) containing RdRP as a minor constituent. In phi6 and other dsRNA bacteriophages from the Cystoviridae family, the inner core is composed of four virus-specific proteins. Of these, protein P2, or Pol subunit, has been tentatively identified as RdRP by sequence comparisons, but the role of this protein in viral RNA synthesis has not been studied until recently. Here, we overview the work on the Pol subunits of phi6 and related viruses from the standpoints of function, structure and evolution.

Original publication

DOI

10.1016/j.virusres.2003.12.005

Type

Journal article

Journal

Virus Res

Publication Date

04/2004

Volume

101

Pages

45 - 55

Keywords

Amino Acid Sequence, Bacteriophage phi 6, Base Sequence, Cystoviridae, Evolution, Molecular, Models, Biological, Models, Molecular, Molecular Sequence Data, Protein Conformation, RNA Replicase, RNA, Viral, Sequence Homology, Amino Acid, Transcription, Genetic