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Nucleic Acids Research, 1993, Vol. 21, No. 19 4621-4626
© 1993

RNA

Encapsidation of heterologous RNAs by bacteriophage MS2 coat protein

Gavin G. Pickett and David S. Peabody*

Department of Cell Biology, University of New Mexico, School of Medicine and Cancer Center Albuquerque, NM 87131, USA

*To whom correspondence should be addressed at

Received May 7, 1993. Revised August 17, 1993. Accepted August 17, 1993.

The RNA bacteriophages of E.coli specifically encapsidate a single copy of the viral genome in a protein shell composed mainly of 180 molecules of coat protein. Coat protein is also a translational repressor and shuts off viral replicase synthesis by interaction with a RNA stem-loop containing the replicase initiation codon. We wondered whether the translational operator also serves as the viral pac site, the signal which mediates the exclusive encapsidation of viral RNA by its interaction with coat protein. To test this idea we measured the ability of lacZ RNA fused to the translational operator to be incorporated into virus-like particles formed from coat protein expressed from a plasmid. The results indicate that the operator-2.urule;acZ RNA is indeed encapsidated and that nucleotide substitutions in the translational operator which reduce the tightness of the coat protein-operator interaction also reduce or abolish encapsidation of the hybrid RNA. When coat protein is expressed in excess compared to the operator-2.urule;acZ RNA, host RNAs are packaged as well. However, elevation of the level of operator-2.urule;acZ RNA relative to coat protein results in its selective encapsidation at the expense of cellular RNAs. Our results are consistent with the proposition that this single protein-RNA interaction accounts both for translational repression and viral genome encapsidation.


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