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Science 30 October 1998:
Vol. 282. no. 5390, pp. 902 - 907
DOI: 10.1126/science.282.5390.902

Research Articles

Force and Velocity Measured for Single Molecules of RNA Polymerase

Michelle D. Wang, * Mark J. Schnitzer, Hong Yin, dagger Robert Landick, Jeff Gelles, Steven M. Block ddagger

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.

dagger    Present address: Department of Physiology, Tufts University Medical School, Boston, MA 02111, USA.

ddagger    To whom correspondence should be addressed. E-mail: block{at}princeton.edu


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