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Structural basis of transcription activation: the CAP-alpha CTD-DNA complex
Author(s): Benoff B, Yang HW, Lawson CL, Parkinson G, Liu JS, Blatter E, Ebright YW, Berman HM, Ebright RH
Source: SCIENCE    Volume: 297    Issue: 5586    Pages: 1562-1566    Published: AUG 30 2002  
Times Cited: 92     References: 49     
Abstract: 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.
Document Type: Article
Language: English
Reprint Address: Berman, HM (reprint author), Rutgers State Univ, Waksman Inst, Piscataway, NJ 08854 USA
Addresses:
1. Rutgers State Univ, Waksman Inst, Piscataway, NJ 08854 USA
2. Rutgers State Univ, Dept Chem, Piscataway, NJ 08854 USA
3. Rutgers State Univ, Howard Hughes Med Inst, Piscataway, NJ 08854 USA
Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 USA
Subject Category: Multidisciplinary Sciences
IDS Number: 588JA
ISSN: 0036-8075
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