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- W1977644920 abstract "DNA polymerase θ protects against genomic instability via an alternative end-joining repair pathway for DNA double-strand breaks. Polymerase θ is overexpressed in breast, lung and oral cancers, and reduction of its activity in mammalian cells increases sensitivity to double-strand break-inducing agents, including ionizing radiation. Reported here are crystal structures of the C-terminal polymerase domain from human polymerase θ, illustrating two potential modes of dimerization. One structure depicts insertion of ddATP opposite an abasic-site analog during translesion DNA synthesis. The second structure describes a cognate ddGTP complex. Polymerase θ uses a specialized thumb subdomain to establish unique upstream contacts to the primer DNA strand, including an interaction with the 3'-terminal phosphate from one of five distinctive insertion loops. These observations demonstrate how polymerase θ grasps the primer to bypass DNA lesions or extend poorly annealed DNA termini to mediate end-joining." @default.
- W1977644920 created "2016-06-24" @default.
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- W1977644920 date "2015-03-16" @default.
- W1977644920 modified "2023-10-15" @default.
- W1977644920 title "Human DNA polymerase θ grasps the primer terminus to mediate DNA repair" @default.
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- W1977644920 doi "https://doi.org/10.1038/nsmb.2993" @default.
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