title: I came to a fork in the DNA and there was RecG.
abstract: RecG is a potent, atypical, monomeric DNA helicase. It simultaneously couples ATP hydrolysis to duplex unwinding and rewinding, and to the displacement of proteins bound to the DNA. A model is presented for the localization of the enzyme to the inner membrane via its binding to SSB. Upon fork stalling, SSB targets the enzyme to the fork where it can act. RecG displays a strong preference for processing the fork in the regression direction, that is, away from the site of damage that initially led to fork arrest. Regression is mediated by strong binding of the wedge domain to the fork arms as well as to parental duplex DNA by the helicase domains. Once RecG has regressed the fork, it will dissociate leaving the now relaxed, Holliday junction-like DNA, available for further processing by enzymes such as RuvAB.
authors.affiliation: Department of Biochemistry, University at Buffalo, Buffalo, NY 14214, USA; Center for Single Molecule Biophysics, University at Buffalo, Buffalo, NY 14214, USA. Electronic address: pbianco@buffalo.edu.
authors.forename: Piero R
authors.initials: PR
authors.lastname: Bianco
mesh_terms: D004247:DNA / Q000737:chemistry* / Q000235:genetics* / Q000648:ultrastructure; D004249:DNA Damage / Q000235:genetics*; D004260:DNA Repair / Q000235:genetics*; D004261:DNA Replication / Q000235:genetics; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics* / Q000648:ultrastructure; D051858:Forkhead Transcription Factors / Q000737:chemistry / Q000235:genetics / Q000648:ultrastructure; D008956:Models, Chemical; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D029968:Escherichia coli Proteins; D051858:Forkhead Transcription Factors; C071446:RecG protein, E coli; D004247:DNA
keywords: DNA helicase; RecG; SSB; recombination; stalled replication fork