5'-Deoxyribose phosphate lyase activity of human DNA polymerase iota in vitro

Science. 2001 Mar 16;291(5511):2156-9. doi: 10.1126/science.1058386.

K Bebenek ¹, A Tissier, E G Frank, J P McDonald, R Prasad, S H Wilson, R Woodgate, T A Kunkel

Affiliations

Affiliation

1 Laboratory of Molecular Genetics and, Laboratory of Structural Biology, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, USA.

PMID: 11251121 DOI: 10.1126/science.1058386

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).

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