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

Abstract : 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.
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Submitted on : Thursday, July 18, 2019 - 11:37:04 AM
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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, Wiley, 2015, 28 (2), pp.117-123. ⟨10.1002/jmr.2435⟩. ⟨hal-02188084⟩

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