Comprehensive ADP-ribosylome analysis identifies tyrosine as an ADP-ribose acceptor site.
Deena M Leslie PedrioliMario LeutertVera BilanKathrin NowakKapila GunasekeraElena FerrariRalph ImhofLars MalmströmMichael O HottigerPublished in: EMBO reports (2018)
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.
Keyphrases
- amino acid
- mass spectrometry
- data analysis
- solar cells
- energy transfer
- multiple sclerosis
- ms ms
- liquid chromatography
- gas chromatography
- emergency department
- optical coherence tomography
- computed tomography
- genome wide
- capillary electrophoresis
- high performance liquid chromatography
- molecular dynamics
- simultaneous determination