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REVIEW: AP Endonuclease 1 as a Key Enzyme in Repair of Apurinic/Apyrimidinic Sites

N. S. Dyrkheeva1, N. A. Lebedeva1,2, and O. I. Lavrik1,2,3*

1Institute of Chemical Biology and Fundamental Medicine, Siberian Division of the Russian Academy of Sciences, 630090 Novosibirsk, Russia

2Novosibirsk State University, 630090 Novosibirsk, Russia

3Altai State University, 656049 Barnaul, Russia; E-mail: lavrik@niboch.nsc.ru

* To whom correspondence should be addressed.

Received June 6, 2016; Revision received June 20, 2016
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.
KEY WORDS: human apurinic/apyrimidinic endonuclease 1 (APE1), AP site, base excision repair, protein–DNA interactions, protein–protein interactions

DOI: 10.1134/S0006297916090042