4.5 Article

Poly(ADP-ribosyl)ation as a new posttranslational modification of YB-1

Journal

BIOCHIMIE
Volume 119, Issue -, Pages 36-44

Publisher

ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.biochi.2015.10.008

Keywords

Y-box binding protein 1 (YB-1); Poly(ADP-ribose)polymerase 1 (PARP1); Poly(ADP-ribose) (PAR pADPr); Multiple DNA lesions; AP endonuclease 1 (APE1)

Funding

  1. Russian Scientific Fund [14-24-00038]
  2. RFBR [13-04-93107]
  3. Program on Molecular and Cell Biology from Presidium of Russian Academy of Sciences

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Multifunctional Y-box binding protein 1 (YB-1) is actively studied as one of the components of cellular response to genotoxic stress. However, the precise role of YB-1 in the process of DNA repair is still obscure. In the present work we report for the first time new posttranslational modification of YB-1 - poly(ADP-ribosyl)ation, catalyzed by one of the main regulatory enzymes of DNA repair - poly(ADPribose)polymerase 1 (PARP1) in the presence of model DNA substrate carrying multiple DNA lesions. Therefore, poly(ADP-ribosyl)ation of YB-1 catalyzed with PARP1, can be stimulated by damaged DNA. The observed property of YB-1 underlines its ability to participate in the DNA repair by its involvement in the regulatory cascades of DNA repair. (C) 2015 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved.

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