Comprehensive ADP-ribosylome analysis identifies tyrosine as an ADP-ribose acceptor site.
| Type | Information |
|---|---|
| Nr | 63 (Research article) |
| Authors | Leslie Pedrioli, Deena; Leutert, Mario; Bilan, Vera; Nowak, Kathrin; Gunasekera, Kapila; Ferrari, Elena; Imhof, Ralph; Malmström, Lars; Hottiger, Michael |
| Title | Comprehensive ADP-ribosylome analysis identifies tyrosine as an ADP-ribose acceptor site. |
| Journal | EMBO Rep (2018) 19(8) e45310 |
| DOI | 10.15252/embr.201745310 |
| Citations | 92 citations (journal impact: 3.22) |
| Abstract | Despite recent mass spectrometry MS-based breakthroughs comprehensive ADP-ribose ADPr-acceptor amino acid identification and ADPr-site localization remain challenging. Here we report the establishment of an unbiased multistep ADP-ribosylome data analysis workflow that led to the identification of tyrosine as a novel ARTD1PARP1-dependent in vivo ADPr-acceptor amino acid. MS analyses of in vitro ADP-ribosylated proteins confirmed tyrosine as an ADPr-acceptor amino acid in RPS3A Y155 and HPF1 Y238 and demonstrated that trans-modification of RPS3A is dependent on HPF1. We provide an ADPr-site Localization Spectra Database ADPr-LSD which contains 288 high-quality ADPr-modified peptide spectra to serve as ADPr spectral references for correct ADPr-site localizations. |