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J Mol Recognit. 2015 Feb;28(2):117-23. doi: 10.1002/jmr.2435. Epub 2015 Jan 21.

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

Author information

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

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 single-stranded 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 mechanism to prevent single-stranded intermediates of DNA replication, transcription and repair from being converted into highly genotoxic DNA strand breaks, thus allowing the cell to coordinate different DNA processing mechanisms.

KEYWORDS:

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

PMID:
25605055
DOI:
10.1002/jmr.2435
[Indexed for MEDLINE]

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