Structural basis of transcription activation: the CAP-alpha CTD-DNA complex.
The Escherichia coli catabolite activator protein (CAP) activates transcription at P(lac), P(gal), and other promoters through interactions with the RNA polymerase alpha subunit carboxyl-terminal domain (alphaCTD). We determined the crystal structure of the CAP-alphaCTD-DNA complex at a resolution of 3.1 angstroms. CAP makes direct protein-protein interactions with alphaCTD, and alphaCTD makes direct protein-DNA interactions with the DNA segment adjacent to the DNA site for CAP. There are no large-scale conformational changes in CAP and alphaCTD, and the interface between CAP and alphaCTD is small. These findings are consistent with the proposal that activation involves a simple "recruitment" mechanism.
Waksman Institute and Department of Chemistry, Howard Hughes Medical Institute, Rutgers University, Piscataway, NJ 08854, USA.
Brian
B
Benoff
Huanwang
H
Yang
Catherine L
CL
Lawson
Gary
G
Parkinson
Jinsong
J
Liu
Erich
E
Blatter
Yon W
YW
Ebright
Helen M
HM
Berman
Richard H
RH
Ebright
D018360:Crystallography, X-Ray; D002373:Cyclic AMP Receptor Protein / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D046911:Macromolecular Substances; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D014158:Transcription, Genetic; D015533:Transcriptional Activation
D002373:Cyclic AMP Receptor Protein; D046911:Macromolecular Substances; D004247:DNA; D012321:DNA-Directed RNA Polymerases; C113275:RNA polymerase alpha subunit