Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 383, Issue 3, Pages 529-538Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2008.08.082
Keywords
bacteriophage; dsRNA virus; in vitro assembly; virus assembly; minor capsid protein
Categories
Funding
- Academy of Finland Centre of Excellence Program 2006-2011 in Virus Research [1213467]
- European Commission's Sixth Framework Program [ERAS-CT-2003-980409]
- Academy of Finland [1112244]
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The polymerase complexes of double-stranded RNA (dsRNA) viruses are multifunctional RNA processing machineries that carry out viral genome packaging, replication, and transcription. The polymerase complex forms the innermost virion shell and is structurally related in dsRNA viruses infecting a diversity of host organisms. In this study, we analyzed the properties and functions of the minor polymerase complex protein P7 of dsRNA bacteriophage phi 6 using terminally truncated P7 polypeptides and an in vitro self-assembly system established for the phi 6 polymerase complex. The N-terminally truncated P7 failed to dimerize, whereas C-terminally truncated P7 polypeptides formed functional dimers that were incorporated into the polymerase complex. Nevertheless, the polymerase complex assembly kinetics and stability were altered by the incorporation of the C-terminally truncated P7. Using the in vitro assembly system for phi 6 nucleocapsids and subsequent infectivity assays, we confirmed that full-length P7 is necessary for the formation of infectious viral particles. Contrary to previous results, we found that P7 must be incorporated into polymerase complexes during shell assembly. (C) 2008 Elsevier Ltd. All rights reserved.
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