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Science 16 March 2001:
Vol. 291. no. 5511, pp. 2156 - 2159
DOI: 10.1126/science.1058386

Reports

5'-Deoxyribose Phosphate Lyase Activity of Human DNA Polymerase &igr; 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 &igr;) is one of several recently discovered DNA polymerases in mammalian cells whose function is unknown. We report here that human pol &igr; 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 &igr; can use its dRP lyase and polymerase activities to repair Gbullet U and Abullet U pairs in DNA. These data and three distinct catalytic properties of pol &igr; 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


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