Force and Velocity Measured for Single Molecules of RNA Polymerase

TLDR

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 RNAP force‑velocity curves differ from those of myosin or kinesin, showing that low‑load biochemical steps do not produce movement, while high loads can halt RNAP by inducing a structural shift that moves the enzyme backward 5–10 base pairs, contradicting earlier models that linked force directly to single‑base translocation.

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.