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Regulation of the Escherichia coli glyA gene by the purR gene product

Journal of BacteriologyPublished 1 July 1990Open access
John G. Steiert, Ronda J. Rolfes, H Zalkin, George V. Stauffer
Citations50
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TL;DR

The purine regulon repressor protein, PurR, was shown to be a purine component involved in glyA regulation in Escherichia coli, and a 24-base-pair region was protected from DNase I digestion by PurR.

Abstract

The purine regulon repressor protein, PurR, was shown to be a purine component involved in glyA regulation in Escherichia coli. Expression of glyA, encoding serine hydroxymethyltransferase activity, was elevated in a purR mutant compared with a wild-type strain. When the purR mutant was transformed with a plasmid carrying the purR gene, the serine hydroxymethyltransferase levels returned to the wild-type level. The PurR protein bound specifically to a DNA fragment carrying the glyA control region, as determined by gel retardation. In a DNase I protection assay, a 24-base-pair region was protected from DNase I digestion by PurR. The glyA operator sequence for PurR binding is similar to that reported for several pur regulon genes.

Keywords

Materials ScienceBiochemistry, Genetics and Molecular Biology