Proteome-Wide Identification of In Vivo ADP-Ribose Acceptor Sites by Liquid Chromatography-Tandem Mass Spectrometry

Methods Mol Biol. 2017:1608:149-162. doi: 10.1007/978-1-4939-6993-7_11.

Abstract

ADP-ribosylation is a posttranslational modification (PTM) that affects a variety of cellular processes. In recent years, mass spectrometry (MS)-based proteomics has become a valuable tool for studying ADP-ribosylation. However, studying this PTM in vivo in an unbiased and sensitive manner has remained a difficult challenge. Here, we describe a detailed protocol for unbiased analysis of ADP-ribosylated proteins and their ADP-ribose acceptor sites under physiological conditions. The method relies on the enrichment of mono-ADP-ribosylated peptides using the macrodomain Af1521 in combination with liquid chromatography-high-resolution tandem MS (LC-MS/MS). The 5-day protocol explains the step-by-step enrichment and identification of ADP-ribosylated peptides from cell culture stage all the way through to data processing using the MaxQuant software suite.

Keywords: ADP-ribosylation; ADP-ribosylome; Af1521 macrodomain enrichment; Affinity purification; Mass spectrometry; PARG; Proteomics.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate Ribose / metabolism*
  • Animals
  • Chromatography, Liquid / methods*
  • Humans
  • Protein Processing, Post-Translational / genetics
  • Protein Processing, Post-Translational / physiology
  • Proteome / metabolism
  • Proteomics / methods
  • Software
  • Tandem Mass Spectrometry / methods*

Substances

  • Proteome
  • Adenosine Diphosphate Ribose