Y-box-binding protein 1 stimulates abasic site cleavage
- Authors: Alemasova E.E.1, Naumenko K.N.1,2, Moor N.A.1, Lavrik O.I.1,2
-
Affiliations:
- Institute of Chemical Biology and Fundamental Medicine
- Novosibirsk State University
- Issue: Vol 82, No 12 (2017)
- Pages: 1521-1528
- Section: Regular Article
- URL: https://journals.rcsi.science/0006-2979/article/view/151541
- DOI: https://doi.org/10.1134/S0006297917120112
- ID: 151541
Cite item
Abstract
Apurinic/apyrimidinic (AP) sites are among the most frequent DNA lesions. The first step in the AP site repair involves the magnesium-dependent enzyme AP endonuclease 1 (APE1) that catalyzes hydrolytic cleavage of the DNA phosphodiester bond at the 5′ side of the AP site, thereby generating a single-strand DNA break flanked by the 3′-OH and 5′-deoxyribose phosphate (dRP) groups. Increased APE1 activity in cancer cells might correlate with tumor chemoresistance to DNA-damaging treatment. It has been previously shown that the multifunctional oncoprotein Y-box-binding protein 1 (YB-1) interacts with APE1 and inhibits APE1-catalyzed hydrolysis of AP sites in single-stranded DNAs. In this work, we demonstrated that YB-1 stabilizes the APE1 complex with double-stranded DNAs containing the AP sites and stimulates cleavage of these AP sites at low magnesium concentrations.
About the authors
E. E. Alemasova
Institute of Chemical Biology and Fundamental Medicine
Email: lavrik@niboch.nsc.ru
Russian Federation, Novosibirsk, 630090
K. N. Naumenko
Institute of Chemical Biology and Fundamental Medicine; Novosibirsk State University
Email: lavrik@niboch.nsc.ru
Russian Federation, Novosibirsk, 630090; Novosibirsk, 630090
N. A. Moor
Institute of Chemical Biology and Fundamental Medicine
Email: lavrik@niboch.nsc.ru
Russian Federation, Novosibirsk, 630090
O. I. Lavrik
Institute of Chemical Biology and Fundamental Medicine; Novosibirsk State University
Author for correspondence.
Email: lavrik@niboch.nsc.ru
Russian Federation, Novosibirsk, 630090; Novosibirsk, 630090