uvrB-dependent, recF-independent post-replication (or replication) repair in Escherichia coli.
In UV-damaged cells, a large fraction of pyrimidine dimers may remain unexcised and may be tolerated by a uvrB recA lexA-dependent non-excisional mode of repair (M. Sedliaková, J. Brozmanová, F. Maŝek and K. Kleibl, Biophys. J., 36 (1981) 429-441). We show here that a similar repair pathway operates in the Escherichia coli recF 143 single mutant but not in the recF uvrB double mutant. This indicates that the putative repair pathway is recF independent.
Slezáriková
V
V
Cancer Research Institute, Slovak Academy of Sciences, Department of Molecular Genetics, Bratislava, Czechoslovakia.
Sedliaková
M
M
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D003562:Cytidine / Q000494:pharmacology; D004265:DNA Helicases; D004260:DNA Repair; D004261:DNA Replication; D004269:DNA, Bacterial / Q000235:genetics / Q000528:radiation effects*; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D004307:Dose-Response Relationship, Radiation; D004926:Escherichia coli / Q000187:drug effects / Q000235:genetics / Q000254:growth & development / Q000528:radiation effects*; D029968:Escherichia coli Proteins; D007700:Kinetics; D011740:Pyrimidine Dimers; D014466:Ultraviolet Rays
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D011740:Pyrimidine Dimers; C058093:UvrB protein, E coli; C489340:recF protein, E coli; D003562:Cytidine; C066218:recF protein, Bacteria; D004265:DNA Helicases