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Comprehensive ADP-ribosylome analysis identifies tyrosine as an ADP-ribose acceptor site.


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.

SUBMITTER: Leslie Pedrioli DM 

PROVIDER: S-EPMC6073207 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature

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Comprehensive ADP-ribosylome analysis identifies tyrosine as an ADP-ribose acceptor site.

Leslie Pedrioli Deena M DM   Leutert Mario M   Bilan Vera V   Nowak Kathrin K   Gunasekera Kapila K   Ferrari Elena E   Imhof Ralph R   Malmström Lars L   Hottiger Michael O MO  

EMBO reports 20180628 8


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 <i>in vivo</i> ADPr-acceptor amino acid. MS analyses of <i>in vitro</i> ADP-ribosylated proteins confirmed tyrosine as an ADPr-acceptor amino acid in RPS  ...[more]

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