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Journal of Virology, December 1998, p. 10058-10065, Vol. 72, No. 12
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Mutational Analysis of the Role of Nucleoside Triphosphatase P4 in the Assembly of the RNA Polymerase Complex of Bacteriophage phi 6

Anja O. Paatero,1 Leonard Mindich,2 and Dennis H. Bamford1,*

Department of Biosciences, Biocenter, FIN-00014, University of Helsinki, Finland,1 and Department of Microbiology, The Public Health Research Institute, New York, New York 100162

Received 31 March 1998/Accepted 25 August 1998

Bacteriophage phi 6 is a complex enveloped double-stranded RNA virus with a segmented genome and replication strategy quite similar to that of the Reoviridae. An in vitro packaging and replication system using purified components is available. The positive-polarity genomic segments are translocated into a preformed polymerase complex (procapsid) particle. This particle is composed of four proteins: the shell-forming protein P1, the RNA polymerase P2, and two proteins active in packaging. Protein P7 is involved in stable packaging, and protein P4 is a homomultimeric potent nucleoside triphosphatase that provides the energy for the RNA translocation event. In this investigation, we used mutational analysis to study P4 multimerization and assembly. P4 is assembled onto a preformed particle containing proteins P2 and P7 in addition to P1. Only simultaneous production of P1 and P4 in the same cell leads to P4 assembly on P1 alone, whereas the P1 shell is incompetent for accepting P4 if produced separately. The C-terminal part of P4 is essential for particle assembly but not for multimerization or enzymatic activity. Altering the P4 nucleoside triphosphate binding site destroys the ability to form multimers.

* Corresponding author. Mailing address: Biocenter 2, P.O. Box 56 (Viikinkaari 5), FIN-00014 University of Helsinki, Finland. Phone: 358-9-70859100. Fax: 358-9-70859098. E-mail: gen_phag{at}cc.helsinki.fi.

Journal of Virology, December 1998, p. 10058-10065, Vol. 72, No. 12
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Yang, H., Makeyev, E. V., Butcher, S. J., Gaidelyte, A., Bamford, D. H. (2002). Two Distinct Mechanisms Ensure Transcriptional Polarity in Double-Stranded RNA Bacteriophages. J. Virol. 77: 1195-1203 [Abstract] [Full Text]  
  • Pirttimaa, M. J., Paatero, A. O., Frilander, M. J., Bamford, D. H. (2002). Nonspecific Nucleoside Triphosphatase P4 of Double-Stranded RNA Bacteriophage {phi}6 Is Required for Single-Stranded RNA Packaging and Transcription. J. Virol. 76: 10122-10127 [Abstract] [Full Text]  
  • Mindich, L. (1999). Precise Packaging of the Three Genomic Segments of the Double-Stranded-RNA Bacteriophage phi 6. Microbiol. Mol. Biol. Rev. 63: 149-160 [Abstract] [Full Text]  


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