Controlling the motor activity of a transcription-repair coupling factor: autoinhibition and the role of RNA polymerase.

ABSTRACT: Motor proteins that couple ATP hydrolysis to movement along nucleic acids play a variety of essential roles in DNA metabolism. Often these enzymes function as components of macromolecular complexes, and DNA translocation by the motor protein drives movement of other components of the complex. In order to understand how the activity of motor proteins is regulated within multi-protein complexes we have studied the bacterial transcription-repair coupling factor, Mfd, which is a helicase superfamily 2 member that binds to RNA polymerase (RNAP) and removes stalled transcription complexes from DNA. Using an oligonucleotide displacement assay that monitors protein movement on double-stranded DNA we show that Mfd has little motor activity in isolation, but exhibits efficient oligonucleotide displa

SUBMITTER: Smith AJ 

PROVIDER: S-EPMC1874598 | biostudies-literature | 2007

REPOSITORIES: biostudies-literature