Deoxyribophosphate lyase activity of mammalian endonuclease VIII-like proteins

被引：21

作者：

Grin, Inga R. ^{[1
]}

Khodyreva, Svetlana N. ^{[1
]}

Nevinsky, Georgy A. ^{[1
]}

Zharkov, Dmitry O. ^{[1
]}

机构：

[1] Russian Acad Sci, SB, Inst Chem Biol & Fundamental Med, Novosibirsk 630090, Russia

来源：

FEBS LETTERS | 2006年 / 580卷 / 20期

基金：

英国惠康基金;

关键词：

DNA repair; base excision; deoxyribophosphate lyase; NEIL; DNA polymerase beta;

D O I：

10.1016/j.febslet.2006.08.011

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Base excision repair (BER) protects cells from nucleobase DNA damage. In eukaryotic BER, DNA glycosylases generate abasic sites, which are then converted to deoxyribo-5'-phosphate (dRP) and excised by a dRP lyase (dRPase) activity of DNA polymerase P (Polo). Here, we demonstrate that NEIL1 and NEIL2, mammalian homologs of bacterial endonuclease VIII, excise dRP by beta-elimination with the efficiency similar to Pol beta. DNA duplexes imitating BER intermediates after insertion of a single nucleotide were better substrates. NEIL1 and NEIL2 supplied dRPase activity in BER reconstituted with dRPase-null Pol beta. Our results suggest a role for NEILs as backup dRPases in mammalian cells. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：4916 / 4922

页数：7

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