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Nucleic Acids Research, 1991, Vol. 19, No. 23 6499-6503
© 1991

MOLECULAR BIOLOGY

RNA binding properties of the coat protein from bacteriophage GA

Jonatha M. Gott+, Larry J. Wilhelm§ and C. Uhlenbeck Olke*

Departments of Chemistry and Biochemistry, University of Colorado Boulder, CO 80309, USA

*To whom correspondence should be addressed

Received August 20, 1991. Accepted November 6, 1991.

The coat protein of bacteriophage GA, a group II RNA phage, binds to a small RNA hairpin corresponding to its replicase operator. Binding is specific, with a Ka of 71 µM–1 This interaction differs kinetically from the analogous coat protein-RNA hairpin interactions of other RNA phage and also deviates somewhat in its pH and salt dependence. Despite 46 of 129 amino acid differences between the GA and group I phage R17 coat proteins, the binding sites are fairly similar. The essential features of the GA coat protein binding site are a based-paired stem with an unpaired purine and a four nucleotide loop having an A at position –4 and a purine at –7 . Unlike the group I phage proteins, the GA coat protein does not distinguish between two alternate positions for the unpaired purine and does not show high specificity for a pyrimidine at position –5 of the loop.

+Present address: Department of Molecular Biology and Microbiology, School of Medicine, Case Western Reserve, Cleveland, OH 44106

§Present address: Synergen, Inc., Boulder, CO, USA


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