AP endonuclease 1 as a key enzyme in repair of apurinic/apyrimidinic sites
- Authors: Dyrkheeva N.S.1, Lebedeva N.A.1,2, Lavrik O.I.1,2,3
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Affiliations:
- Institute of Chemical Biology and Fundamental Medicine
- Novosibirsk State University
- Altai State University
- Issue: Vol 81, No 9 (2016)
- Pages: 951-967
- Section: Review
- URL: https://journals.rcsi.science/0006-2979/article/view/150999
- DOI: https://doi.org/10.1134/S0006297916090042
- ID: 150999
Cite item
Abstract
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.
About the authors
N. S. Dyrkheeva
Institute of Chemical Biology and Fundamental Medicine
Email: lavrik@niboch.nsc.ru
Russian Federation, Novosibirsk, 630090
N. A. Lebedeva
Institute of Chemical Biology and Fundamental Medicine; Novosibirsk State University
Email: lavrik@niboch.nsc.ru
Russian Federation, Novosibirsk, 630090; Novosibirsk, 630090
O. I. Lavrik
Institute of Chemical Biology and Fundamental Medicine; Novosibirsk State University; Altai State University
Author for correspondence.
Email: lavrik@niboch.nsc.ru
Russian Federation, Novosibirsk, 630090; Novosibirsk, 630090; Barnaul, 656049