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Nucleic Acids Research, 1994, Vol. 22, No. 18 3748-3752
© 1994

RNA

Mutations that increase the affinity of a translational repressor for RNA

Francis Lim and S.Peabody David*

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

*To whom correspondence should be addressed

Received May 23, 1994. Revised July 14, 1994. Accepted July 14, 1994.

The coat protein of the RNA bacteriophage MS2 is a specific RNA binding protein that represses translation of the viral replicase gene during the infection cycle. As an approach to characterizing the RNA-binding site of coat protein we have isolated a series of coat mutants that suppress the effects of a mutation in the translational operator. Each of the mutants exhibits a super-repressor phenotype, more tightly repressing both the mutant and wild-type operators than does the wild-type protein. The variant coat proteins were purified and subjected to filter binding assays to determine their affinities for the mutant and wild-type operators. Each protein binds the operators from 3 to 7.5-fold more tightly than normal coat protein. The amino acid substitutions seem to extend the normal binding site by introducing new interactions with RNA.


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