Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1864, Issue 12, Pages 1631-1640Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/J.bbapap.2016.08.012
Keywords
Y-box binding protein 1 (YB-1); RNA; Base excision repair (BER) regulation; PARP1(2); Poly(ADP-ribose) (PAR)
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Funding
- RSF [14-24-00038]
- Russian Federation
- Russian Science Foundation [14-24-00038] Funding Source: Russian Science Foundation
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Base excision repair (BER) is a flagship DNA repair system responsible for maintaining genome integrity. Apart from basal enzymes, this system involves several accessory factors essential for coordination and regulation of DNA processing during substrate channeling. Y-box-binding protein 1 (YB-1), a multifunctional factor that can interact with DNA, RNA, poly(ADP-ribose) and plenty of proteins including DNA repair enzymes, is increasingly considered as a non-canonical protein of BER. Here we provide quantitative characterization of YB-1 physical interactions with key BER factors such as PARPI, PARP2, APEI, NEIL1 and pol beta and comparison of the full-length YB-1 and its C-terminally truncated nuclear form in regard to their binding affinities for BER proteins. Data on functional interactions reveal strong stimulation of PARP1 autopoly(ADP-ribosyl)ation and inhibition of poly(ADP-ribose) degradation by PARG in the presence of YB-1. Moreover, YB-1 is shown to stimulate AP lyase activity of NEIL1 and to inhibit dRP lyase activity of pol beta on model DNA duplex structure. We also demonstrate for the first time YB-1 poly(ADP-ribosyl)ation in the presence of RNA. (C) 2016 Elsevier B.V. All rights reserved.
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