GcvA-mediated activation of gcvT-lacZ expression involves the carboxy-terminal domain of the alpha subunit of RNA polymerase.
Several LysR-type transcriptional regulators have been shown to require the carboxy-terminal domain of the alpha subunit (alphaCTD) of RNA polymerase to activate their target genes. We show here that GcvA, a LysR-type protein, also uses the alphaCTD to activate the Escherichia coli gcvTHP operon. Amino acid residues in the alphaCTD important for GcvA-dependent activation, however, have no effect on GcvA-mediated repression of the operon.
Jourdan
A D
AD
Department of Microbiology, University of Iowa, Iowa City, IA 52242, USA.
Stauffer
G V
GV
D050960:Aminomethyltransferase; D001426:Bacterial Proteins / Q000502:physiology; D012321:DNA-Directed RNA Polymerases / Q000235:genetics / Q000502:physiology*; D004926:Escherichia coli / Q000201:enzymology; D029968:Escherichia coli Proteins; D005786:Gene Expression Regulation; D019877:Hydroxymethyl and Formyl Transferases / Q000378:metabolism*; D007763:Lac Operon / Q000235:genetics; D009154:Mutation; D012097:Repressor Proteins / Q000502:physiology; D014157:Transcription Factors
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C095455:GcvR protein, E coli; D012097:Repressor Proteins; D014157:Transcription Factors; D019877:Hydroxymethyl and Formyl Transferases; D050960:Aminomethyltransferase; D012321:DNA-Directed RNA Polymerases; C113275:RNA polymerase alpha subunit