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PMID: 9794753 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Force and velocity measured for single molecules of RNA polymerase.

Science (New York, N.Y.) ·Vol. 282 ·No. 5390 ·1998-10-30 ·Pages 902-7

Wang MD, Schnitzer MJ, Yin H, Landick R, Gelles J, Block SM

Abstract

RNA polymerase (RNAP) moves along DNA while carrying out transcription, acting as a molecular motor. Transcriptional velocities for single molecules of Escherichia coli RNAP were measured as progressively larger forces were applied by a feedback-controlled optical trap. The shapes of RNAP force-velocity curves are distinct from those of the motor enzymes myosin or kinesin, and indicate that biochemical steps limiting transcription rates at low loads do not generate movement. Modeling the data suggests that high loads may halt RNAP by promoting a structural change which moves all or part of the enzyme backwards through a comparatively large distance, corresponding to 5 to 10 base pairs. This contrasts with previous models that assumed force acts directly upon a single-base translocation step.

MeSH Terms
DNA, Bacterial/metabolism DNA-Directed RNA Polymerases/chemistry,metabolism Escherichia coli/enzymology Mathematics Models, Chemical Molecular Motor Proteins/chemistry,metabolism RNA, Bacterial/biosynthesis RNA, Messenger/biosynthesis Templates, Genetic Thermodynamics Transcription, Genetic
Chemicals
DNA, Bacterial Molecular Motor Proteins RNA, Bacterial RNA, Messenger DNA-Directed RNA Polymerases
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Wang M D
Department of Molecular Biology and Princeton Materials Institute, Princeton University, Princeton, NJ 08544, USA.
Schnitzer M J
Yin H
Landick R
Gelles J
Block S M
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1998-10-30
Pages
902-7
Language
English
Region
United States
NLM ID
0404511
Subset
IM
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