AP endonuclease 1 as a key enzyme in repair of apurinic/apyrimidinic sites

被引:30
作者
Dyrkheeva, N. S. [1 ]
Lebedeva, N. A. [1 ,2 ]
Lavrik, O. I. [1 ,2 ,3 ]
机构
[1] Russian Acad Sci, Inst Chem Biol & Fundamental Med, Siberian Div, Novosibirsk 630090, Russia
[2] Novosibirsk State Univ, Novosibirsk 630090, Russia
[3] Altai State Univ, Barnaul 656049, Russia
基金
俄罗斯科学基金会;
关键词
human apurinic/apyrimidinic endonuclease 1 (APE1); AP site; base excision repair; protein-DNA interactions; protein-protein interactions; BASE-EXCISION-REPAIR; DNA-POLYMERASE-BETA; HUMAN APURINIC ENDONUCLEASE; HUMAN 8-OXOGUANINE-DNA GLYCOSYLASE; REPLICATION PROTEIN-A; ABASIC SITE; POLY(ADP-RIBOSE) POLYMERASE-1; EXONUCLEASE ACTIVITY; FLAP ENDONUCLEASE-1; MAMMALIAN-CELLS;
D O I
10.1134/S0006297916090042
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
Human apurinic/apyrimidinic endonuclease 1 (APE1) is one of the key participants in the DNA base excision repair system. APE1 hydrolyzes DNA adjacent to the 5'-end of an apurinic/apyrimidinic (AP) site to produce a nick with a 3'-hydroxyl group and a 5'-deoxyribose phosphate moiety. APE1 exhibits 3'-phosphodiesterase, 3'-5'-exonuclease, and 3-phosphatase activities. APE1 was also identified as a redox factor (Ref-1). In this review, data on the role of APE1 in the DNA repair process and in other metabolic processes occurring in cells are analyzed as well as the interaction of this enzyme with DNA and other proteins participating in the repair system.
引用
收藏
页码:951 / 967
页数:17
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