Inhibition of abasic site cleavage in bubble DNA by multifunctional protein YB-1

Elizaveta Fomina (1) , Pavel Pestryakov (1) , Dmitry Kretov (2, 3) , Dmitry Zharkov (4, 1) , Lev Ovchinnikov (3) , Patrick A. Curmi (2) , Olga Lavrik (1, 4, 5)

1 ICBFM SB RAS - Institute of Chemical Biology and Fundamental Medicine [Novosibirsk, Russia]
2 SABNP - Structure et activité des biomolécules normales et pathologiques
3 Institute of Protein Research, Russian Academy of Sciences, Pushchino
4 NSU - Novosibirsk State University
5 Altai State University

Y-box binding protein 1 (YB-1) is widely known to participate in a multiple DNA and RNA processing events in the living cell. YB-1 is also regarded as a putative component of DNA repair. This possibility is supported by relocalization of YB-1 into the nucleus following genotoxic stress. Increased affinity of YB-1 for damaged DNA, especially in its singlestranded form, and its functional interaction with proteins responsible for the initiation of apurinic/apyrimidinic (AP) site repair, namely, AP endonuclease 1 and DNA glycosylase NEIL1, suggest that YB-1 could be involved in the repair of AP sites as a regulatory protein. Here we show that YB-1 has a significant inhibitory effect on the cleavage of AP sites located in single-stranded DNA and in DNA bubble structures. Such interference may be considered as a possible mechanismto prevent single-stranded intermediates of DNA replication, transcription and repair frombeing converted into highly genotoxic DNA strand breaks, thus allowing the cell to coordinate different DNA processing mechanisms.

Keywords: AP endonuclease 1 (APE1); NEIL1; Y-box binding protein 1 (YB-1); DNA repair; abasic site (AP site)

Domains: Life Sciences [q-bio]

Elizaveta Fomina, Pavel Pestryakov, Dmitry Kretov, Dmitry Zharkov, Lev Ovchinnikov, et al.. Inhibition of abasic site cleavage in bubble DNA by multifunctional protein YB-1. Journal of Molecular Recognition, 2015, 28 (2), pp.117-123. ⟨10.1002/jmr.2435⟩. ⟨hal-02188084⟩