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

Elizaveta Alemasova (1) , Pavel Pestryakov (1) , Maria Sukhanova (1, 2) , Dmitry Kretov (3, 4) , Nina Moor (1, 2) , Patrick A. Curmi (4) , Lev Ovchinnikov (3) , Olga Lavrik (1, 2)

1 ICBFM SB RAS - Institute of Chemical Biology and Fundamental Medicine [Novosibirsk, Russia]
2 Université d'État de Novossibirsk
3 Institute of Protein Research, Russian Academy of Sciences, Pushchino
4 SABNP - Structure et activité des biomolécules normales et pathologiques

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(ADP-ribose)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.

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

Domains: Life Sciences [q-bio]

Elizaveta Alemasova, Pavel Pestryakov, Maria Sukhanova, Dmitry Kretov, Nina Moor, et al.. Poly(ADP-ribosyl)ation as a new posttranslational modification of YB-1. Biochimie, 2015, 119, pp.36-44. ⟨10.1016/j.biochi.2015.10.008⟩. ⟨hal-02272805⟩