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EMBO Rep. 2018 Aug;19(8). pii: e45310. doi: 10.15252/embr.201745310. Epub 2018 Jun 28.

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

Author information

1
Department of Molecular Mechanisms of Disease, University of Zurich, Zurich, Switzerland.
2
Molecular Life Science PhD Program of the Life Science Zurich Graduate School, Zurich, Switzerland.
3
S3IT and Institute for Computational Science, University of Zurich, Zurich, Switzerland.
4
Department of Molecular Mechanisms of Disease, University of Zurich, Zurich, Switzerland michael.hottiger@dmmd.uzh.ch.

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.

KEYWORDS:

ADP‐ribosylation; ARTD1/PARP1; HPF1; genotoxic stress; tyrosine ADP‐ribosylation

PMID:
29954836
PMCID:
PMC6073207
DOI:
10.15252/embr.201745310
[Indexed for MEDLINE]
Free PMC Article

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