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

Elizaveta E Alemasova; Pavel E Pestryakov; Maria V Sukhanova; Dmitry A Kretov; Nina A Moor; Patrick A Curmi; Lev P Ovchinnikov; Olga I Lavrik

doi:10.1016/j.biochi.2015.10.008

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

Biochimie. 2015 Dec:119:36-44. doi: 10.1016/j.biochi.2015.10.008. Epub 2015 Oct 9.

Authors

Elizaveta E Alemasova¹, Pavel E Pestryakov¹, Maria V Sukhanova², Dmitry A Kretov³, Nina A Moor², Patrick A Curmi⁴, Lev P Ovchinnikov⁵, Olga I Lavrik⁶

Affiliations

¹ Institute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk, 630090, Russia.
² Institute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk, 630090, Russia; Novosibirsk State University, Novosibirsk, 630090, Russia.
³ Institute of Protein Research, RAS, Pushchino, Moscow Region, 142290, Russia; Institut National de la Santé et de la Recherche Médicale (INSERM), UMR 829, Université d'Evry Val d'Essonne, Laboratoire Structure-Activité des Biomolécules Normales et Pathologiques, Evry, 91025, France.
⁴ Institut National de la Santé et de la Recherche Médicale (INSERM), UMR 829, Université d'Evry Val d'Essonne, Laboratoire Structure-Activité des Biomolécules Normales et Pathologiques, Evry, 91025, France.
⁵ Institute of Protein Research, RAS, Pushchino, Moscow Region, 142290, Russia.
⁶ Institute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk, 630090, Russia; Novosibirsk State University, Novosibirsk, 630090, Russia. Electronic address: lavrik@niboch.nsc.ru.

PMID: 26453809
DOI: 10.1016/j.biochi.2015.10.008

Abstract

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).

Publication types

Comparative Study
Research Support, Non-U.S. Gov't

MeSH terms

DNA / metabolism
DNA Breaks, Double-Stranded
DNA Damage*
DNA Repair*
Electrophoretic Mobility Shift Assay
Humans
Isoenzymes / genetics
Isoenzymes / metabolism
Kinetics
Models, Biological*
Mutation
NAD / metabolism
Oxidative Stress
Peptide Fragments / chemistry
Peptide Fragments / genetics
Peptide Fragments / metabolism
Poly (ADP-Ribose) Polymerase-1 / genetics
Poly (ADP-Ribose) Polymerase-1 / metabolism*
Poly Adenosine Diphosphate Ribose / metabolism
Poly(ADP-ribose) Polymerases / genetics
Poly(ADP-ribose) Polymerases / metabolism
Protein Processing, Post-Translational*
Recombinant Proteins / chemistry
Recombinant Proteins / metabolism
Saccharomyces cerevisiae Proteins / genetics
Saccharomyces cerevisiae Proteins / metabolism
Up-Regulation*
Y-Box-Binding Protein 1 / chemistry
Y-Box-Binding Protein 1 / genetics
Y-Box-Binding Protein 1 / metabolism*

Substances

Isoenzymes
Peptide Fragments
Recombinant Proteins
Saccharomyces cerevisiae Proteins
Y-Box-Binding Protein 1
YBX1 protein, human
NAD
Poly Adenosine Diphosphate Ribose
DNA
calf thymus DNA
PARP1 protein, human
PARP2 protein, S cerevisiae
Poly (ADP-Ribose) Polymerase-1
Poly(ADP-ribose) Polymerases