Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 52, Pages 44945-44951Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M111.299347
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Funding
- National Institutes of Health [P01 CA77852, T32 AI007411]
- NCI [R01 GM41712]
- NIAID
- American Cancer Society [PF-10-083-01]
- Hillcrest Committee of Southern Oregon
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MRE11-RAD50 is a highly conserved multifunctional DNA repair factor. Here, we show that MRE11-RAD50 cleaves the covalent 3'-phosphotyrosyl-DNA bonds that join topoisomerase 1 (Top1) to the DNA backbone and that are the hallmark of damage caused by Top1 poisons such as camptothecin. Cleavage generates a 3'-phosphate DNA end that MRE11-RAD50 can resect in an ATP-regulated reaction, to produce a 3'-hydroxyl that can prime repair synthesis. The 3'-phosphotyrosyl cleavage activity maps to the MRE11 active site. These results define a new activity of MRE11 and distinguish MRE11-RAD50 functions in repair of Top1-DNA complexes and double-strand breaks.
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