The role of the N-terminal domain of human apurinic/apyrimidinic endonuclease 1, APE1, in DNA glycosylase stimulation
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The N-terminal domain of human APE1 is shown to be essential for stimulating DNA glycosylases (OGG1, MBD4, ANPG). Electron microscopy reveals APE1 oligomerization along DNA with helix distortions that enhance enzyme–substrate interactions and turnover, particularly on short duplexes—suggesting a mechanism that facilitates efficient base excision repair.
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Kladova, O.A.; Bazlekowa-Karaban, M.; Baconnais, S.; Piétrement, O.; Ishchenko, A.A.; Matkarimov, B.T.; Iakovlev, D.A.; Vasenko, A.; Fedorova, O.S.; Le Cam, E.; Tudek, B.; Kuznetsov, N.A.; Saparbaev, M. (2018). The role of the N-terminal domain of human apurinic/apyrimidinic endonuclease 1, APE1, in DNA glycosylase stimulation. DNA Repair, 64, 10–25. DOI: 10.1016/j.dnarep.2018.02.001