Investigation of bacterial nucleotide excision repair using single-molecule techniques.
Despite three decades of biochemical and structural analysis of the prokaryotic nucleotide excision repair (NER) system, many intriguing questions remain with regard to how the UvrA, UvrB, and UvrC proteins detect, verify and remove a wide range of DNA lesions. Single-molecule techniques have begun to allow more detailed understanding of the kinetics and action mechanism of this complex process. This article reviews how atomic force microscopy and fluorescence microscopy have captured new glimpses of how these proteins work together to mediate NER.
Department of Pharmacology and Chemical Biology, University of Pittsburgh Cancer Institute, University of Pittsburgh, Pittsburgh, PA, USA. Electronic address: vanhoutenb@upmc.edu.
Bennett
B
Van Houten
School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, UK.
Neil
N
Kad
D000595:Amino Acid Sequence; D001407:Bacillus / Q000737:chemistry / Q000201:enzymology / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001483:Base Sequence; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D004265:DNA Helicases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004260:DNA Repair; D045643:DNA Repair Enzymes / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008856:Microscopy, Fluorescence; D008969:Molecular Sequence Data
D001426:Bacterial Proteins; D004247:DNA; D004265:DNA Helicases; D045643:DNA Repair Enzymes
Bacterial nucleotide excision repair; Single molecule; UvrA; UvrB; UvrC; UvrD