| Chapter title |
Identification of ADP-Ribose Acceptor Sites on In Vitro Modified Proteins by Liquid Chromatography–Tandem Mass Spectrometry
|
|---|---|
| Chapter number | 10 |
| Book title |
Poly(ADP-Ribose) Polymerase
|
| Published in |
Methods in molecular biology, July 2017
|
| DOI | 10.1007/978-1-4939-6993-7_10 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-6992-0, 978-1-4939-6993-7
|
| Authors |
Mario Leutert, Vera Bilan, Peter Gehrig, Michael O. Hottiger |
| Abstract |
Protein ADP-ribosylation is a covalent, reversible posttranslational modification (PTM) catalyzed by ADP-ribosyltransferases (ARTs). Proteins can be either mono- or poly-ADP-ribosylated under a variety of physiological and pathological conditions. To understand the functional contribution of protein ADP-ribosylation to normal and disease/stress states, modified protein and corresponding ADP-ribose acceptor site identification is crucial. Since ADP-ribosylation is a transient and relatively low abundant PTM, systematic and accurate identification of ADP-ribose acceptor sites has only recently become feasible. This is due to the development of specific ADP-ribosylated protein/peptide enrichment methodologies, as well as technical advances in high-accuracy liquid chromatography-tandem mass spectrometry (LC-MS/MS). The standardized protocol described here allows the identification of ADP-ribose acceptor sites in in vitro ADP-ribosylated proteins and will, thus, contribute to the functional characterization of this important PTM. |
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