Opening and Closing of the Bacterial RNA Polymerase Clamp

Author:

Chakraborty Anirban1,Wang Dongye1,Ebright Yon W.1,Korlann You2,Kortkhonjia Ekaterine12,Kim Taiho3,Chowdhury Saikat4,Wigneshweraraj Sivaramesh5,Irschik Herbert6,Jansen Rolf6,Nixon B. Tracy4,Knight Jennifer7,Weiss Shimon2,Ebright Richard H.1

Affiliation:

1. Howard Hughes Medical Institute, Waksman Institute, and Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ 08854, USA.

2. Department of Chemistry and Biochemistry, University of California at Los Angeles, Los Angeles, CA 90095, USA.

3. Nesher Technologies, Inc., 2100 West Third Street, Los Angeles, CA 90057, USA.

4. Department of Biochemistry, Pennsylvania State University, State College, PA 16802, USA.

5. Centre for Molecular Microbiology and Infection, Imperial College London, London SW7 2AZ, UK.

6. Helmholtz Centre for Infection Research, 38124 Braunschweig, Germany.

7. Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.

Abstract

Clamping Down Crystal structures of RNA polymerase show that a “clamp” region which surrounds the DNA binding site can adopt conformations ranging from a closed to an open state. Chakraborty et al. (p. 591 ) used single-molecule fluorescence energy transfer experiments to detect the clamp's conformational changes in solution during the transcription cycle. The results support a model in which a clamp opening allows DNA to be loaded into the active-center cleft and unwound. Direct interactions with DNA likely trigger clamp closure upon formation of a catalytically competent transcription initiation complex.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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