Research Article

Force and Velocity Measured for Single Molecules of RNA Polymerase

See allHide authors and affiliations

Science  30 Oct 1998:
Vol. 282, Issue 5390, pp. 902-907
DOI: 10.1126/science.282.5390.902

You are currently viewing the abstract.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution


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.

  • * 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}

View Full Text