MetR-mediated repression of the glyA gene in Escherichia coli.
Inactivation of either of the two MetR binding sites centered at bp -143 and 121 relative to the +1 transcription start site results in reduced glyA-lacZ expression in a wild-type strain below the level seen in a metR mutant. This reduced expression is dependent on the side of the DNA helix MetR binds relative to the RNA polymerase binding site. Thus, a single MetR dimer bound to the DNA may play a physiological role in maintaining appropriate glyA gene expression, functioning as a repressor under low MetR conditions.
Department of Microbiology, University of Iowa, Iowa City 52242, USA.
E
E
Lorenz
G V
GV
Stauffer
D001426:Bacterial Proteins / Q000235:genetics / Q000502:physiology*; D004790:Enzyme Induction; D004926:Escherichia coli / Q000235:genetics*; D015964:Gene Expression Regulation, Bacterial; D012696:Glycine Hydroxymethyltransferase / Q000096:biosynthesis* / Q000235:genetics; D008715:Methionine / Q000378:metabolism; D016296:Mutagenesis; D011401:Promoter Regions, Genetic / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012097:Repressor Proteins / Q000235:genetics / Q000502:physiology*; D015534:Trans-Activators / Q000235:genetics / Q000502:physiology*
D001426:Bacterial Proteins; C058169:MetR protein, Bacteria; D011993:Recombinant Fusion Proteins; D012097:Repressor Proteins; D015534:Trans-Activators; D008715:Methionine; D012696:Glycine Hydroxymethyltransferase