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Science 30 October 1998: Vol. 282. no. 5390, pp. 902 - 907 DOI: 10.1126/science.282.5390.902
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Research Articles
Force and Velocity Measured for Single Molecules of RNA Polymerase
Michelle D. Wang,
*
Mark J. Schnitzer,
Hong Yin,
Robert Landick,
Jeff Gelles,
Steven M. Block
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.
M. D. Wang and S. M. Block, Department of Molecular
Biology and Princeton Materials Institute, Princeton University,
Princeton, NJ 08544, USA. M. J. Schnitzer, Departments of Physics
and Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
H. Yin and J. Gelles, Department of Biochemistry, Brandeis University,
Waltham, MA 02254, USA. R. Landick, Department of Bacteriology,
University of Wisconsin, Madison, WI 53706, USA.
*
Present address: Department of Physics, Cornell University, Ithaca, NY
14853, USA.
Present address: Department of Physiology, Tufts University
Medical School, Boston, MA 02111, USA.
To whom correspondence should be addressed. E-mail:
block{at}princeton.edu
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