5'-Deoxyribose Phosphate Lyase Activity of Human DNA Polymerase ɩ in Vitro-Reference-Cited by-同舟云学术

5'-Deoxyribose Phosphate Lyase Activity of Human DNA Polymerase ɩ in Vitro

Published:2001-03-16 Issue:5511 Volume:291 Page:2156-2159
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Bebenek Katarzyna¹,Tissier Agnès²,Frank Ekaterina G.²,McDonald John P.²,Prasad Rajendra³,Wilson Samuel H.³,Woodgate Roger²,Kunkel Thomas A.¹³

Affiliation:

1. Laboratory of Molecular Genetics and

2. Section on DNA Replication, Repair and Mutagenesis, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892–2725, USA.

3. Laboratory of Structural Biology, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, USA.

Abstract

DNA polymerase iota (pol ι) is one of several recently discovered DNA polymerases in mammalian cells whose function is unknown. We report here that human pol ι 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 ι 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 ι implicate it in specialized forms of base excision repair (BER).

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference31 articles.

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