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Journal of Bacteriology, August 2003, p. 4572-4577, Vol. 185, No. 15
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.15.4572-4577.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Isolation and Analysis of Mutants of Double-Stranded-RNA Bacteriophage {phi}6 with Altered Packaging Specificity

Jian Qiao, Xueying Qiao, Yang Sun, and Leonard Mindich*

Department of Microbiology, Public Health Research Institute, Newark, New Jersey 07103

Received 20 March 2003/ Accepted 9 May 2003

The genomes of bacteriophage {phi}6 and its relatives are packaged through a mechanism that involves the recognition and translocation of the three different plus strand transcripts of the segmented double-stranded RNA genomes into preformed polyhedral structures called procapsids or inner cores. This packaging requires hydrolysis of nucleoside triphosphates and takes place in the order S-M-L. Packaging is dependent on unique sequences of about 200 nucleotides near the 5' ends of plus strand transcripts of the three genomic segments. Changes in the pac sequences lead to loss of packaging ability but can be suppressed by second-site changes in RNA or amino acid changes in protein P1, the major structural protein of the procapsid. It appears that P1 is the determinant of the RNA binding sites, and it is suggested that the binding sites overlap or are conformational changes of the same domains.

* Corresponding author. Mailing address: Public Health Research Institute, 225 Warren St., Newark, NJ 07103. Phone: (973) 854-3420. Fax: (973) 854-3421. E-mail: mindich{at}phri.org.

Journal of Bacteriology, August 2003, p. 4572-4577, Vol. 185, No. 15
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.15.4572-4577.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Sen, A., Heymann, J. B., Cheng, N., Qiao, J., Mindich, L., Steven, A. C. (2008). Initial Location of the RNA-dependent RNA Polymerase in the Bacteriophage {Phi}6 Procapsid Determined by Cryo-electron Microscopy. J. Biol. Chem. 283: 12227-12231 [Abstract] [Full Text]  


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