UvrABC protein

Dependence of Nucleotide Excision Repair by E. coli UvrABC Proteins on Adduct Conformation... 

B., and Geadntov, N.E. (2007) Sequence context- and temperature-dependent nucleotide exdsion repair of a benzojo] pyrene diol epoxide-guanine DNA addud catalyzed by thermophilic UvrABC proteins. Biochemistry, 46, 7006-7015. 

Goosen, N., Moolenaar, G. F., Visse, R., and van de Putte, P. (1998). Functional domains of the E. coli UvrABC proteins in nucleotide excision repair. In Nucleic Acids and Molecular Biology DNA Repair (F. Eckstein and D. M. J. Lilley, Eds.), pp. 103-123. Springer, Berlin. 

Very recently, it has been observed that E. coli produces UvrABC excision repair proteins, and that the UvrAB complex binds to the convex side of a cisplatin-induced kink in DNA (205) It would be of great interest to study the similarities between this complex and the DRP protein mentioned above. 

One of the best-understood examples of nucleotide-excision repair is the excision of a pyrimidine dimer. Three enzymatic activities are essential for this repair process in E. coli (Figure 27.49). First, an enzyme complex consisting of the proteins encoded by the uvrABC genes detects the distortion produced by the pyrimidine dimer. A specific uvrABC... 

NER in bacteria involves only three proteins to carry out the complete process of damage recognition and excision UvrA, UvrB, and UvrC. Owing to its relative simplicity, the UvrABC system has been studied extensively, particularly in E. coli, and serves as a model system for NER [20, 21]. 

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