An N-terminal clamp restrains the motor domains of the bacterial transcription-repair coupling factor Mfd.

ABSTRACT: Motor proteins that translocate on nucleic acids are key players in gene expression and maintenance. While the function of these proteins is diverse, they are driven by highly conserved core motor domains. In transcription-coupled DNA repair, motor activity serves to remove RNA polymerase stalled on damaged DNA, making the lesion accessible for repair. Structural and biochemical data on the bacterial transcription-repair coupling factor Mfd suggest that this enzyme undergoes large conformational changes from a dormant state to an active state upon substrate binding. Mfd can be functionally dissected into an N-terminal part instrumental in recruiting DNA repair proteins (domains 1-3, MfdN), and a C-terminal part harboring motor activity (domains 4-7, MfdC). We show that isolated MfdC has el

SUBMITTER: Murphy MN 

PROVIDER: S-EPMC2764443 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature