| Literature DB >> 29954836 |
Deena M Leslie Pedrioli1, Mario Leutert1,2, Vera Bilan1, Kathrin Nowak1,2, Kapila Gunasekera1, Elena Ferrari1, Ralph Imhof1, Lars Malmström3, Michael O Hottiger4.
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 ARTD1/PARP1-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.Entities:
Keywords: ADP‐ribosylation; ARTD1/PARP1; HPF1; genotoxic stress; tyrosine ADP‐ribosylation
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Year: 2018 PMID: 29954836 PMCID: PMC6073207 DOI: 10.15252/embr.201745310
Source DB: PubMed Journal: EMBO Rep ISSN: 1469-221X Impact factor: 8.807