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Nucleic Acids Research, 1988, Vol. 16, No. 3 997-1010
© 1988

Articles

Affinities of ribosomal protein S20 and C-terminal deletion mutants for 16S rRNA and S20 mRNA

B.Cameron Donly and George A. Mackie*

Department of Biochemistry, University of Western Ontario London, Ontario N6A 5C1, Canada

*To whom correspondence should be addressed

Received September 28, 1987. Accepted December 22, 1987.

We have measured the binding of E. coli ribosomal protein S20 and a number of C-terminal deletion mutants to 16S rRNA and in vitro transcribed S20 mRNA. Mutant S20s of interest were synthesized in vitro from the appropriate plasmid templates by coupled transcription and translation. The of S20 produced in vitro for 16S rRNA is 1.2 x 107 (M–1) in a gel filtration assay. Removal of as few as 6 residue8 from the C terminus of S20 results in a sharp loss of binding activity, suggesting the presence of critical residues in this region. Analysis of the amino acid sequence of S20 indicates that these residues may constitute part of a segment of {alpha} helix. Although S20 is known to autoregulate its own synthesis, we were unable to demonstrate any measurable affinity of S20 for its own mRNA.


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