Architectural requirements for optimal activation by tandem CRP molecules at a class I CRP-dependent promoter.
The Escherichia coli cyclic AMP receptor protein (CRP) activates transcription at target promoters by interacting with the C-terminal domain of the RNA polymerase alpha subunit. We have constructed a set of promoters carrying tandem DNA sites for CRP with one site centred at position -61.5 and the other site located at different upstream positions. Optimal CRP-dependent activation of transcription is observed when the upstream DNA site for CRP is located at position -93.5 or at position -103.5. Evidence is presented to suggest that activation by the upstream-bound CRP molecule is due to interaction with the C-terminal domain of the RNA polymerase alpha subunit.
Tebbutt
John
J
School of Biosciences, University of Birmingham, Edgbaston, B15 2TT, UK.
Rhodius
Virgil A
VA
Webster
Christine L
CL
Busby
Stephen J W
SJ
D001426:Bacterial Proteins / Q000378:metabolism*; D001483:Base Sequence; D002352:Carrier Proteins; D000242:Cyclic AMP / Q000378:metabolism; D002373:Cyclic AMP Receptor Protein / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism; D008969:Molecular Sequence Data; D011401:Promoter Regions, Genetic; D021122:Protein Subunits; D016415:Sequence Alignment; D012689:Sequence Homology, Nucleic Acid
D001426:Bacterial Proteins; D002352:Carrier Proteins; D002373:Cyclic AMP Receptor Protein; D021122:Protein Subunits; D000242:Cyclic AMP; D012321:DNA-Directed RNA Polymerases