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Science 30 August 2002:
Vol. 297. no. 5586, pp. 1562 - 1566
DOI: 10.1126/science.1076376
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Reports

Structural Basis of Transcription Activation: The CAP-alpha CTD-DNA Complex

Brian Benoff,1 Huanwang Yang,1 Catherine L. Lawson,1 Gary Parkinson,1* Jinsong Liu,1dagger Erich Blatter,12ddagger Yon W. Ebright,12 Helen M. Berman,1§ Richard H. Ebright12parallel

The Escherichia coli catabolite activator protein (CAP) activates transcription at Plac, Pgal, and other promoters through interactions with the RNA polymerase alpha  subunit carboxyl-terminal domain (alpha CTD). We determined the crystal structure of the CAP-alpha CTD-DNA complex at a resolution of 3.1 angstroms. CAP makes direct protein-protein interactions with alpha CTD, and alpha CTD 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 alpha CTD, and the interface between CAP and alpha CTD is small. These findings are consistent with the proposal that activation involves a simple "recruitment" mechanism.

1 Waksman Institute and Department of Chemistry,
2 Howard Hughes Medical Institute, Rutgers University, Piscataway, NJ 08854, USA.
*   Present address: CRC Biomolecular Structure Unit, Institute of Cancer Research, London SW3 6JB, UK.

dagger    Present address: Tularik Inc., South San Francisco, CA 94080, USA.

ddagger    Present address: Human Genome Sciences Inc., Rockville, MD 20874, USA.

§   To whom correspondence on crystallographic issues should be addressed. E-mail: berman{at}rutchem.rutgers.edu

parallel    To whom correspondence on all other issues should be addressed. E-mail: ebright{at}mbcl.rutgers.edu

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