Mechanism of genome instability mediated by human DNA polymerase mu misincorporation.

Guo, Miao; Wang, Yina; Tang, Yuyue; Chen, Zijing; Hou, Jinfeng; Dai, Jingli; Wang, Yudong; Wang, Liangyan et al. · Nat Commun · 2021

basic_science · Level V

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Abstract

Pol μ is capable of performing gap-filling repair synthesis in the nonhomologous end joining (NHEJ) pathway. Together with DNA ligase, misincorporation of dGTP opposite the templating T by Pol μ results in a promutagenic T:G mispair, leading to genomic instability. Here, crystal structures and kinetics of Pol μ substituting dGTP for dATP on gapped DNA substrates containing templating T were determined and compared. Pol μ is highly mutagenic on a 2-nt gapped DNA substrate, with T:dGTP base pairing at the 3' end of the gap. Two residues (Lys438 and Gln441) interact with T:dGTP and fine tune the active site microenvironments. The in-crystal misincorporation reaction of Pol μ revealed an unexpected second dGTP in the active site, suggesting its potential mutagenic role among human X family polymerases in NHEJ.

Medical subject headings