Catabolite activator protein: DNA binding and transcription activation.
Recently determined structures of the Escherichia coli catabolite activator protein (CAP) in complex with DNA, and in complex with the RNA polymerase alpha subunit C-terminal domain (alphaCTD) and DNA, have yielded insights into how CAP binds DNA and activates transcription. Comparison of multiple structures of CAP-DNA complexes has revealed the contributions of direct and indirect readout to DNA binding by CAP. The structure of the CAP-alphaCTD-DNA complex has provided the first structural description of interactions between a transcription activator and its functional target within the general transcription machinery. Using the structure of the CAP-alphaCTD-DNA complex, the structure of an RNA polymerase-DNA complex, and restraints from biophysical, biochemical and genetic experiments, it has been possible to construct detailed three-dimensional models of intact class I and class II transcription activation complexes.
Lawson
Catherine L
CL
Department of Chemistry and Chemical Biology, Rutgers University, 610 Taylor Road, Piscataway, NJ 08854, USA. cathy.lawson@rutgers.edu
Swigon
David
D
Murakami
Katsuhiko S
KS
Darst
Seth A
SA
Berman
Helen M
HM
Ebright
Richard H
RH
D002373:Cyclic AMP Receptor Protein / Q000378:metabolism*; D004247:DNA / Q000235:genetics / Q000378:metabolism*; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism*; D004926:Escherichia coli; D008957:Models, Genetic; D008958:Models, Molecular; D011401:Promoter Regions, Genetic / Q000235:genetics; D013329:Structure-Activity Relationship; D015533:Transcriptional Activation / Q000235:genetics*
D002373:Cyclic AMP Receptor Protein; D004247:DNA; D012321:DNA-Directed RNA Polymerases; C113275:RNA polymerase alpha subunit