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Structural basis of transcription activation: the CAP-alpha CTD-DNA complex.

Benoff B., Yang H., Lawson C.L., Parkinson G., Liu J., Blatter E., Ebright Y.W., Berman H.M., Ebright R.H.

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.

Science 297:1562-1566(2002) [PubMed] [Europe PMC]

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