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- W2891409523 abstract "Summary CtIP is involved in the resection of double-stranded DNA breaks during the S and G2 phases of the cell cycle for repair by homologous recombination. Acting in concert with the MRN complex, it plays a particularly important role in handling complex DNA end structures by localised nucleolytic processing of DNA termini in preparation for longer range resection. Here we show that human CtIP is a tetrameric protein adopting a dumbbell architecture in which DNA binding domains are connected by long coiled-coils. The protein complex binds two short DNA duplexes with high affinity and bridges DNA molecules in trans . DNA binding is potentiated by dephosphorylation and is not specific for DNA end structures per se . However, the affinity for linear DNA molecules is increased if the DNA terminates with more complex structures including forked ssDNA overhangs and model nucleoprotein conjugates. This work provides a biochemical and structural basis for the function of CtIP at complex DNA breaks." @default.
- W2891409523 created "2018-09-27" @default.
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- W2891409523 date "2018-09-05" @default.
- W2891409523 modified "2023-09-23" @default.
- W2891409523 title "Human CtIP forms a tetrameric dumbbell-shaped particle which binds and bridges complex DNA end structures for double-strand break repair" @default.
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- W2891409523 doi "https://doi.org/10.1101/409102" @default.
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