Header

UZH-Logo

Maintenance Infos

Comprehensive ADP‐ribosylome analysis identifies tyrosine as an ADP‐ribose acceptor site


Leslie Pedrioli, Deena M; Leutert, Mario; Bilan, Vera; Nowak, Kathrin; Gunasekera, Kapila; Ferrari, Elena; Imhof, Ralph; Malmström, Lars; Hottiger, Michael O (2018). Comprehensive ADP‐ribosylome analysis identifies tyrosine as an ADP‐ribose acceptor site. EMBO Reports, 19(8):e45310.

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.

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.

Statistics

Citations

Dimensions.ai Metrics
23 citations in Web of Science®
22 citations in Scopus®
Google Scholar™

Altmetrics

Downloads

0 downloads since deposited on 09 Aug 2018
0 downloads since 12 months

Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:05 Vetsuisse Faculty > Department of Molecular Mechanisms of Disease
07 Faculty of Science > Department of Molecular Mechanisms of Disease
Dewey Decimal Classification:570 Life sciences; biology
Scopus Subject Areas:Life Sciences > Biochemistry
Life Sciences > Molecular Biology
Life Sciences > Genetics
Uncontrolled Keywords:DP‐ribosylation, ARTD1/PARP1, HPF1, genotoxic stress, tyrosine ADP‐ribosylation
Language:English
Date:28 June 2018
Deposited On:09 Aug 2018 15:12
Last Modified:29 Jul 2020 07:28
Publisher:Nature Publishing Group
ISSN:1469-221X
OA Status:Closed
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:https://doi.org/10.15252/embr.201745310
PubMed ID:29954836
Project Information:
  • : FunderSNSF
  • : Grant ID31003A_176177
  • : Project TitleUncovering the function of cell stress-associated ADP-ribosylomes
  • : FunderSNSF
  • : Grant ID310030_157019
  • : Project TitleRole of mono-ADP-ribosylhydrolases in inflammatory signaling

Download

Closed Access: Download allowed only for UZH members