Abstract
DNA polymerase iota (pol iota) is one of several recently discovered DNA polymerases in mammalian cells whose function is unknown. We report here that human pol iota has an intrinsic 5'-deoxyribose phosphate (dRP) lyase activity. In reactions reconstituted with uracil-DNA glycosylase (UDG), apurinic/apyrimidinic (AP) endonuclease and DNA ligase I, pol iota can use its dRP lyase and polymerase activities to repair G*U and A*U pairs in DNA. These data and three distinct catalytic properties of pol iota implicate it in specialized forms of base excision repair (BER).
MeSH terms
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Amino Acid Sequence
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Base Pairing
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Base Sequence
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Carbon-Oxygen Lyases / metabolism
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DNA / metabolism*
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DNA Glycosylases*
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DNA Ligase ATP
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DNA Ligases / metabolism
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DNA Polymerase iota
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DNA Repair*
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DNA-(Apurinic or Apyrimidinic Site) Lyase
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DNA-Directed DNA Polymerase / chemistry
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DNA-Directed DNA Polymerase / metabolism*
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Deoxyribonuclease IV (Phage T4-Induced)
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Humans
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Molecular Sequence Data
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N-Glycosyl Hydrolases / metabolism
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Phosphorus-Oxygen Lyases / metabolism*
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Recombinant Fusion Proteins / metabolism
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Ribosemonophosphates / metabolism*
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Schiff Bases
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Uracil / metabolism
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Uracil-DNA Glycosidase
Substances
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LIG1 protein, human
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Recombinant Fusion Proteins
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Ribosemonophosphates
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Schiff Bases
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Uracil
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5-deoxyribose 1-phosphate
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DNA
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5'-deoxyribose phosphate lyase
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DNA-Directed DNA Polymerase
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Deoxyribonuclease IV (Phage T4-Induced)
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DNA Glycosylases
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N-Glycosyl Hydrolases
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Uracil-DNA Glycosidase
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Carbon-Oxygen Lyases
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DNA-(Apurinic or Apyrimidinic Site) Lyase
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Phosphorus-Oxygen Lyases
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DNA Ligases
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DNA Ligase ATP
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DNA Polymerase iota
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POLI protein, human