Poly(ADP-ribosyl)ation as a new posttranslational modification of YB-1
Autor: | Elizaveta E. Alemasova, Nina A. Moor, Lev P. Ovchinnikov, Maria V. Sukhanova, Dmitry A. Kretov, P. E. Pestryakov, Olga I. Lavrik, Patrick A. Curmi |
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Přispěvatelé: | Institute of Chemical Biology and Fundamental Medicine [Novosibirsk, Russia] (ICBFM SB RAS), Siberian Branch of the Russian Academy of Sciences (SB RAS), Université d'État de Novossibirsk, Institute of Protein Research, Russian Academy of Sciences, Pushchino, Structure et activité des biomolécules normales et pathologiques (SABNP), Université d'Évry-Val-d'Essonne (UEVE)-Institut National de la Santé et de la Recherche Médicale (INSERM), Maciejak, Olek |
Rok vydání: | 2015 |
Předmět: |
Poly Adenosine Diphosphate Ribose
Saccharomyces cerevisiae Proteins HMG-box DNA Repair DNA repair DNA polymerase Poly ADP ribose polymerase DNA polymerase II [SDV]Life Sciences [q-bio] Y-box binding protein 1 (YB-1) Poly (ADP-Ribose) Polymerase-1 Electrophoretic Mobility Shift Assay Biochemistry Models Biological Humans DNA Breaks Double-Stranded AP endonuclease 1 (APE1) DNA clamp biology Multiple DNA lesions General Medicine Base excision repair DNA NAD Peptide Fragments Recombinant Proteins Proliferating cell nuclear antigen Up-Regulation [SDV] Life Sciences [q-bio] Isoenzymes Kinetics Oxidative Stress Poly(ADP-ribose)polymerase 1 (PARP1) Mutation biology.protein pADPr) Y-Box-Binding Protein 1 Poly(ADP-ribose) (PAR Poly(ADP-ribose) Polymerases Protein Processing Post-Translational DNA Damage |
Zdroj: | Biochimie Biochimie, Elsevier, 2015, 119, pp.36-44. ⟨10.1016/j.biochi.2015.10.008⟩ Biochimie, 2015, 119, pp.36-44. ⟨10.1016/j.biochi.2015.10.008⟩ |
ISSN: | 1638-6183 0300-9084 |
Popis: | International audience; 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. |
Databáze: | OpenAIRE |
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