4.5 Article

Role of polymerase β in complementing aprataxin deficiency during abasic-site base excision repair

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NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 21, 期 5, 页码 497-499

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NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2818

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  1. Intramural Research Program of the US National Institutes of Health, National Institute of Environmental Health Sciences [Z01 ES050158, ES050159]

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DNA polymerase beta (pol beta) lyase removal of 5'-deoxyribose phosphate (5'-dRP) from base excision repair (BER) intermediates is critical in mammalian BER involving the abasic site. We found that pol beta also removes 5'-adenylated dRP from BER intermediates after abortive ligation. The crystal structure of a human pol beta-DNA complex showed the 5'-AMP-dRP group positioned in the lyase active site. Pol beta expression rescued methyl methanesulfonate sensitivity in aprataxin (hnt3)- and FEN1 (rad27)-deficient yeast.

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