The molecular mechanism of transcription-coupled DNA repair.
DNA damage that blocks the transcription of genes is prioritized for repair by transcription-coupled DNA repair pathways. RNA polymerases stalled at DNA lesions obstruct repair enzymes, but this situation is turned to the advantage of the cell by transcription-repair coupling factors that remove the stalled RNA polymerase from DNA and increase the rate at which the lesion is repaired. Recent structural studies of the bacterial transcription-repair coupling factor, Mfd, have revealed a modular architecture in which an ATP-dependent DNA-based motor is coupled to protein-protein interaction domains that can attach the motor to RNA polymerase and the DNA repair protein UvrA. Here I review the key features of this multifunctional protein and discuss how recent mechanistic and structural findings have advanced our understanding of transcription-coupled DNA repair in bacteria.
Savery
Nigel J
NJ
DNA-Protein Interactions Unit, Department of Biochemistry, University of Bristol, Bristol BS8 1TD, UK. n.j.savery@bris.ac.uk
D001419:Bacteria / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry / Q000502:physiology*; D004249:DNA Damage; D004260:DNA Repair / Q000235:genetics / Q000502:physiology*; D012321:DNA-Directed RNA Polymerases / Q000502:physiology; D005827:Genetics, Microbial; D017434:Protein Structure, Tertiary; D014157:Transcription Factors / Q000737:chemistry / Q000502:physiology*; D014158:Transcription, Genetic
D001426:Bacterial Proteins; D014157:Transcription Factors; C072103:transcription repair coupling factor protein, Bacteria; D012321:DNA-Directed RNA Polymerases