Site-specific characterization of the Asp- and Glu-ADP-ribosylated proteome

Nat Methods. 2013 Oct;10(10):981-4. doi: 10.1038/nmeth.2603. Epub 2013 Aug 18.

Abstract

Poly(ADP-ribosyl)ation is catalyzed by a family of enzymes known as PARPs. We describe a method to characterize the human aspartic acid- and glutamic acid-ADP-ribosylated proteome. We identified 1,048 ADP-ribosylation sites on 340 proteins involved in a wide array of nuclear functions; among these were many previously unknown PARP downstream targets whose ADP-ribosylation was sensitive to PARP inhibitor treatment. We also confirmed that iniparib had a negligible effect on PARP activity in intact cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate Ribose / chemistry*
  • Adenosine Diphosphate Ribose / genetics
  • Adenosine Diphosphate Ribose / metabolism
  • Aspartic Acid / chemistry*
  • Aspartic Acid / metabolism
  • Binding Sites
  • DNA Damage
  • Gene Knockdown Techniques
  • Glutamic Acid / chemistry*
  • Glutamic Acid / metabolism
  • Glycoside Hydrolases / chemistry
  • Glycoside Hydrolases / genetics
  • Glycoside Hydrolases / metabolism
  • HCT116 Cells
  • Humans
  • Hydrogen Peroxide / pharmacology
  • Models, Molecular
  • Poly (ADP-Ribose) Polymerase-1
  • Poly(ADP-ribose) Polymerase Inhibitors
  • Poly(ADP-ribose) Polymerases / chemistry*
  • Poly(ADP-ribose) Polymerases / genetics
  • Poly(ADP-ribose) Polymerases / metabolism
  • Protein Conformation
  • Protein Processing, Post-Translational
  • Proteome / chemistry*
  • Proteome / genetics
  • Proteome / metabolism

Substances

  • Poly(ADP-ribose) Polymerase Inhibitors
  • Proteome
  • Adenosine Diphosphate Ribose
  • Aspartic Acid
  • Glutamic Acid
  • Hydrogen Peroxide
  • PARP1 protein, human
  • Poly (ADP-Ribose) Polymerase-1
  • Poly(ADP-ribose) Polymerases
  • Glycoside Hydrolases