RNA polymerase motions during promoter melting-Reference-Cited by-同舟云学术

RNA polymerase motions during promoter melting

Published:2017-05-26 Issue:6340 Volume:356 Page:863-866
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Feklistov Andrey¹^ORCID,Bae Brian¹^ORCID,Hauver Jesse¹^ORCID,Lass-Napiorkowska Agnieszka²^ORCID,Kalesse Markus³^ORCID,Glaus Florian⁴,Altmann Karl-Heinz⁴^ORCID,Heyduk Tomasz²,Landick Robert⁵⁶^ORCID,Darst Seth A.¹^ORCID

Affiliation:

1. The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA.

2. Edward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, USA.

3. Helmholtz Centre for Infection Research, Inhoffenstraße 7, 38124 Brunswick, Germany.

4. ETH Zürich, Department of Chemistry and Applied Biosciences, Institute of Pharmaceutical Sciences, Vladimir-Prelog-Weg 1-5/10 8093 Zürich, Switzerland.

5. Department of Biochemistry, University of Wisconsin–Madison, Madison, WI 53706, USA.

6. Department of Bacteriology, University of Wisconsin–Madison, Madison, WI 53706, USA.

Abstract

Trapping RNA polymerase in the act The enzyme RNA polymerase (RNAP) finds promoter elements in the genome, separates (or “melts”) the DNA strands, and transcribes the template DNA strand to give RNA. A mobile clamp in RNAP plays a key role in initiating transcription. Feklistov et al. locked the clamp of bacterial RNAP in distinct conformations by using small molecules. They then used fluorescent probes to monitor binding as the promoter DNA was separated. Unexpectedly, they found that the clamp transiently closed to nucleate DNA melting, opened to load single-stranded DNA into the active site, and then closed around the template strand to start transcription. Science , this issue p. 863

Funder

National Institutes of Health

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference46 articles.

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2. Structural Basis for Promoter −10 Element Recognition by the Bacterial RNA Polymerase σ Subunit

3. Structure of a bacterial RNA polymerase holoenzyme open promoter complex

4. Crystal Structures of the E. coli Transcription Initiation Complexes with a Complete Bubble

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