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Nucleic Acids Research 2004 32(12):3515-3521; doi:10.1093/nar/gkh680
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Published online 6 July 2004

Nucleic Acids Research, Vol. 32 No. 12 © Oxford University Press 2004; all rights reserved

Packaging motor from double-stranded RNA bacteriophage {phi}12 acts as an obligatory passive conduit during transcription

Denis E. Kainov, Jirí Lísal, Dennis H. Bamford and Roman Tuma*

Institute of Biotechnology and Faculty of Biological Science, Viikki Biocenter, University of Helsinki, PO Box 65, Viikinkaari 1, Helsinki FIN-00014, Finland

* To whom correspondence should be addressed. Tel: +358 9 19159577; Fax: +358 9 19159930; Email: roman.tuma{at}helsinki.fi

Received April 8, 2004; Revised June 4, 2004; Accepted June 16, 2004

Double-stranded RNA viruses sequester their genomes within a protein shell, called the polymerase complex. Translocation of ssRNA into (packaging) and out (transcription) of the polymerase complex are essential steps in the life cycle of the dsRNA bacteriophages of the Cystoviridae family ({phi}6–{phi}14). Both processes require a viral molecular motor P4, an NTPase, which bears structural and functional similarities to hexameric helicases. In effect, switching between the packaging and the transcription mode requires the translocation direction of the P4 motor to reverse. However, the mechanism of the reversal remains elusive. Here we characterize the P4 protein from bacteriophage {phi}12 and exploit its purine nucleotide specificity to delineate P4 role in transcription. The results indicate that while P4 actively translocates RNA during packaging it acts as a passive conduit for RNA export. The directionality switching is accomplished via the regulation of P4 NTPase activity within the polymerase core.


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