PMID:17376770
| Citation |
Sinha, KM, Stephanou, NC, Gao, F, Glickman, MS and Shuman, S (2007) Mycobacterial UvrD1 is a Ku-dependent DNA helicase that plays a role in multiple DNA repair events, including double-strand break repair. J. Biol. Chem. 282:15114-25 |
|---|---|
| Abstract |
Mycobacterium tuberculosis and other bacterial pathogens have a Ku-dependent nonhomologous end joining pathway of DNA double-strand break repair. Here we identify mycobacterial UvrD1 as a novel interaction partner for Ku in a genome-wide yeast two-hybrid screen. UvrD1 per se is a vigorous DNA-dependent ATPase but a feeble DNA helicase. Ku stimulates UvrD1 to catalyze ATP-dependent unwinding of 3'-tailed DNAs. UvrD1, Ku, and DNA form a stable ternary complex in the absence of ATP. The Ku binding determinants are located in the distinctive C-terminal segment of UvrD1. A second mycobacterial paralog, UvrD2, is a vigorous Ku-independent DNA helicase. Ablation of UvrD1 sensitizes Mycobacterium smegmatis to killing by ultraviolet and ionizing radiation and to a single chromosomal break generated by I-SceI endonuclease. The physical and functional interactions of bacterial Ku and UvrD1 highlight the potential for cross-talk between components of nonhomologous end joining and nucleotide excision repair pathways. |
| Links |
PubMed Online version:10.1074/jbc.M701167200 |
| Keywords |
Bacterial Proteins/genetics; Bacterial Proteins/metabolism; DNA Breaks, Double-Stranded/radiation effects; DNA Helicases/genetics; DNA Helicases/metabolism; DNA Repair/physiology; DNA Repair/radiation effects; Deoxyribonucleases, Type II Site-Specific/metabolism; Gamma Rays; Mycobacterium smegmatis/enzymology; Mycobacterium smegmatis/genetics; Mycobacterium tuberculosis/enzymology; Mycobacterium tuberculosis/genetics; Protein Binding/physiology; Protein Binding/radiation effects; Protein Structure, Tertiary/physiology; Saccharomyces cerevisiae Proteins; Ultraviolet Rays |
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