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Science 16 March 2001: Vol. 291. no. 5511, pp. 2156 - 2159 DOI: 10.1126/science.1058386
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Reports
5'-Deoxyribose Phosphate Lyase Activity of Human DNA Polymerase in Vitro
Katarzyna Bebenek,1
Agnès Tissier,3
Ekaterina G. Frank,3
John P. McDonald,3
Rajendra Prasad,2
Samuel H. Wilson,2
Roger Woodgate,3
Thomas A. Kunkel12*
DNA polymerase iota (pol ) is one of several recently
discovered DNA polymerases in mammalian cells whose function is
unknown. We report here that human pol 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 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 implicate it in
specialized forms of base excision repair (BER).
1 Laboratory of Molecular Genetics and
2 Laboratory of Structural Biology, National
Institute of Environmental Health Sciences, National Institutes of
Health, Research Triangle Park, NC 27709, USA.
3 Section on DNA Replication, Repair and
Mutagenesis, National Institute of Child Health and Human Development,
National Institutes of Health, Bethesda, MD 20892-2725, USA.
*
To whom correspondence should be addressed. E-mail:
kunkel{at}niehs.nih.gov
Read the Full Text
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