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Inhibition of abasic site cleavage in bubble DNA by multifunctional protein YB‐1
Author(s) -
Fomina Elizaveta E.,
Pestryakov Pavel E.,
Kretov Dmitry A.,
Zharkov Dmitry O.,
Ovchinnikov Lev P.,
Curmi Patrick A.,
Lavrik Olga I.
Publication year - 2015
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.2435
Subject(s) - ap site , dna , dna repair , dna replication , dna damage , dna glycosylase , endonuclease , microbiology and biotechnology , chemistry , replication protein a , biology , ap endonuclease , biochemistry , dna binding protein , transcription factor , gene
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. Copyright © 2015 John Wiley & Sons, Ltd.