哺乳动物类核酸内切酶 VIII 样蛋白的脱氧核糖磷酸裂解酶活性。
Deoxyribophosphate lyase activity of mammalian endonuclease VIII-like proteins.
作者信息
Grin Inga R, Khodyreva Svetlana N, Nevinsky Georgy A, Zharkov Dmitry O
机构信息
SB RAS Institute of Chemical Biology and Fundamental Medicine, Novosibirsk 630090, Russia.
出版信息
FEBS Lett. 2006 Sep 4;580(20):4916-22. doi: 10.1016/j.febslet.2006.08.011. Epub 2006 Aug 15.
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 beta (Polbeta). Here, we demonstrate that NEIL1 and NEIL2, mammalian homologs of bacterial endonuclease VIII, excise dRP by beta-elimination with the efficiency similar to Polbeta. 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 Polbeta. Our results suggest a role for NEILs as backup dRPases in mammalian cells.
碱基切除修复（BER）保护细胞免受核碱基DNA损伤。在真核生物的BER中，DNA糖基化酶产生无碱基位点，然后将其转化为脱氧核糖-5'-磷酸（dRP），并通过DNA聚合酶β（Polβ）的dRP裂解酶（dRPase）活性将其切除。在这里，我们证明细菌内切核酸酶VIII的哺乳动物同源物NEIL1和NEIL2通过β-消除切除dRP，其效率与Polβ相似。插入单个核苷酸后模仿BER中间体的DNA双链体是更好的底物。NEIL1和NEIL2在用无dRPase的Polβ重建的BER中提供dRPase活性。我们的结果表明NEILs在哺乳动物细胞中作为备用dRPases发挥作用。
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