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

By J G Steiert, R J Rolfes, H Zalkin and G V Stauffer

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

Topics: Research Article
Year: 1990
DOI identifier: 10.1128/jb.172.7.3799-3803.1990
OAI identifier: oai:pubmedcentral.nih.gov:213358
Provided by: PubMed Central
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