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

Elizaveta E Alemasova1, Pavel E Pestryakov1, Maria V Sukhanova2

  • 1Institute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk, 630090, Russia.

Biochimie
|October 11, 2015
PubMed

Insights

Y-box binding protein 1 (YB-1) undergoes poly(ADP-ribosyl)ation, a new modification catalyzed by PARP1, especially when DNA is damaged. This finding suggests YB-1 plays a role in DNA repair pathways.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Y-box binding protein 1 (YB-1) is recognized for its role in cellular responses to genotoxic stress.
  • The specific involvement of YB-1 in DNA repair mechanisms remains incompletely understood.

Purpose of the Study:

  • To investigate novel posttranslational modifications of YB-1.
  • To elucidate the potential role of YB-1 in DNA repair processes.

Main Methods:

  • In vitro assays using poly(ADP-ribose)polymerase 1 (PARP1).
  • Employing model DNA substrates with multiple DNA lesions.
  • Analysis of YB-1 poly(ADP-ribosyl)ation.

Main Results:

  • Identified and characterized a new posttranslational modification of YB-1: poly(ADP-ribosyl)ation.
  • Demonstrated that PARP1 catalyzes the poly(ADP-ribosyl)ation of YB-1.
  • Showed that this modification is stimulated by damaged DNA substrates.

Conclusions:

  • YB-1 is subject to poly(ADP-ribosyl)ation, a modification mediated by PARP1.
  • Damaged DNA can enhance the PARP1-catalyzed poly(ADP-ribosyl)ation of YB-1.
  • This newly identified modification highlights YB-1's potential involvement in DNA repair regulatory cascades.
Keywords:
AP endonuclease 1 (APE1)Multiple DNA lesionsPoly(ADP-ribose) (PARPoly(ADP-ribose)polymerase 1 (PARP1)Y-box binding protein 1 (YB-1)pADPr)

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