RNA binding properties of the coat protein from bacteriophage GA

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

25 Scopus citations

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 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.

Original languageEnglish (US)
Pages (from-to)6499-6503
Number of pages5
JournalNucleic acids research
Volume19
Issue number23
DOIs
StatePublished - Dec 11 1991

ASJC Scopus subject areas

  • Genetics

Fingerprint Dive into the research topics of 'RNA binding properties of the coat protein from bacteriophage GA'. Together they form a unique fingerprint.

Cite this