||UvrA, UvrB, and UvrC form complexes that recognize DNA damage, and incise DNA 3' and 5' to damaged lesions in nucleotide excision repair. UvrA-C function according to the scheme below [PUB_0461]:
UvrA2B complex recognizes DNA damage
UvrA hydrolyzes ATP and dissociates from UvrB, leaving a DNA-UvrB complex
UvrC complexes with UvrB, inducing a conformational change in UvrB which nicks the DNA 4 nt 3' to the damage
UvrC nicks the DNA 7 nt 5' to the damage
Sancar and others report kinetic rates in the range kcat=0.08-0.50 1/min [PUB_0767].
Incision catalyzed by UvrABC at rate 0.39 fmol/min by 20 μmol solution containing 10 nM UvrA, 1000 nM UvrB, and 5 nM UvcR [PUB_0515].
Friedberg EC, Walker GC, Siede W, Wood RD, Schultz RA, Ellenberger T. DNA repair and mutagenesis. ASM Press (2006). WholeCell: PUB_0461, ISBN: 9781555813192
Husain I, Van Houten B, Thomas DC, Abdel-Monem M, Sancar A. Effect of DNA polymerase I and DNA helicase II on the turnover rate of UvrABC excision nuclease. Proc Natl Acad Sci U S A 82, 6774-8 (1985). WholeCell: PUB_0767, PubMed: 2931721
Zou Y, Liu TM, Geacintov NE, Van Houten B. Interaction of the UvrABC nuclease system with a DNA duplex containing a single stereoisomer of dG-(+)- or dG-(-)-anti-BPDE. Biochemistry 34, 13582-93 (1995). WholeCell: PUB_0515, PubMed: 7577947