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  • Title: Kinetic analysis of bypass of O(6)- methylguanine by the catalytic core of yeast DNA polymerase eta.
    Author: Liu B, Xue Q, Gu S, Wang W, Chen J, Li Y, Wang C, Zhang H.
    Journal: Arch Biochem Biophys; 2016 Apr 15; 596():99-107. PubMed ID: 26976707.
    Abstract:
    Alkylating agents can form O(6)-methylguansine (O(6)-MeG). To study the intrinsic kinetic behaviors of bypassing O(6)-MeG, we used the catalytic core of yeast DNA polymerase η (Pol ηcore, residues 1-513), instead of the full-length Pol η, to study their elementary steps, eliminating the effects of the C-terminal C2H2 motif on dNTP incorporation. The misincorporation frequencies were 10(-4) for G and 0.055-0.446 for O(6)-MeG. O(6)-MeG does not affect the extension efficiency. Pol ηcore showed no fast burst phase for any incorporation opposite G or O(6)-MeG. Primer extension was greatly blocked by O(6)-MeG and about 67% dTTP, 31% dCTP and 2% dATP were incorporated opposite O(6)-MeG. This study provides further understanding of the mutation mechanism of alkylated lesion for yeast DNA polymerase η.
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