Abstract
DNA polymerase β (pol β) 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 β also removes 5'-adenylated dRP from BER intermediates after abortive ligation. The crystal structure of a human pol β-DNA complex showed the 5'-AMP-dRP group positioned in the lyase active site. Pol β expression rescued methyl methanesulfonate sensitivity in aprataxin (hnt3)- and FEN1 (rad27)-deficient yeast.
Publication types
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Research Support, N.I.H., Intramural
MeSH terms
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Crystallography, X-Ray
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DNA / chemistry
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DNA Polymerase beta / chemistry*
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DNA Polymerase beta / physiology
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DNA Repair*
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DNA-Binding Proteins / chemistry*
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DNA-Binding Proteins / metabolism
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DNA-Binding Proteins / physiology
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Humans
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Models, Molecular
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Nuclear Proteins / chemistry*
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Nuclear Proteins / metabolism
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Nuclear Proteins / physiology
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Protein Structure, Tertiary
Substances
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APTX protein, human
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DNA-Binding Proteins
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Nuclear Proteins
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DNA
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DNA Polymerase beta