PFM39 is a potent cell-permeable Mirin analog that selectively inhibits MRE11 exo-, but not endo-, nuclease activity.
PFM39 is a potent cell-permeable Mirin analog that selectively inhibits MRE11 exo-, but not endo-, nuclease activity. PFM39 targets MRE11 in a fashion similar to Mirin, but distinct from that of PFM01 to allow a blockage of dsDNA phosphate backbone rotation and selective inhibition against MRE11 exo-, but not endo-, nuclease activity. FM39 potently impairs G2-phase double-strand break (DSB) repair in 1BR3-hTERT fibrolasts following ionizing irradiation (IR).
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Repair of DNA double-strand breaks (DSBs) by homologous recombination (HR) is critical for survival and genome stability of individual cells and organisms, but also contributes to the genetic diversity of species. A vital step in HR is MRN-CtIP-dependent end resection
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 34(2), 2812-2820 (2020-01-08)
The Mre11A/RAD50/NBN complex (MRN) is an essential regulator of the cellular damage response after DNA double-strand breaks (DSBs). More recent work has indicated that MRN may also impact on the duration of mitosis. We show here that RAD50-deficient fibroblasts exhibit
MRE11 within the MRE11-RAD50-NBS1 (MRN) complex acts in DNA double-strand break repair (DSBR), detection, and signaling; yet, how its endo- and exonuclease activities regulate DSBR by nonhomologous end-joining (NHEJ) versus homologous recombination (HR) remains enigmatic. Here, we employed structure-based design
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