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. 1991 Dec 11;19(23):6499–6503. doi: 10.1093/nar/19.23.6499

RNA binding properties of the coat protein from bacteriophage GA.

J M Gott 1, L J Wilhelm 1, O C Uhlenbeck 1
PMCID: PMC329206  PMID: 1754387

Abstract

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 microM -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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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