Comprehensive ADP-ribosylome analysis identifies tyrosine as an ADP-ribose acceptor site.
EMBO Rep
; 19(8)2018 08.
Article
en En
| MEDLINE
| ID: mdl-29954836
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.
Palabras clave
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Tirosina
/
Adenosina Difosfato Ribosa
/
ADP-Ribosilación
Tipo de estudio:
Prognostic_studies
Límite:
Humans
Idioma:
En
Año:
2018
Tipo del documento:
Article