全面的 ADP-ribosylome 分析鉴定酪氨酸为 ADP-核糖受体位点。
Comprehensive ADP-ribosylome analysis identifies tyrosine as an ADP-ribose acceptor site.
机构信息
Department of Molecular Mechanisms of Disease, University of Zurich, Zurich, Switzerland.
Molecular Life Science PhD Program of the Life Science Zurich Graduate School, Zurich, Switzerland.
出版信息
EMBO Rep. 2018 Aug;19(8). doi: 10.15252/embr.201745310. Epub 2018 Jun 28.
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 ADPr-acceptor amino acid. MS analyses of ADP-ribosylated proteins confirmed tyrosine as an ADPr-acceptor amino acid in RPS3A (Y155) and HPF1 (Y238) and demonstrated that -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.
摘要
尽管最近在质谱（MS）技术方面取得了突破，但全面鉴定 ADP-核糖（ADPr）接受氨基酸和 ADPr 位点定位仍然具有挑战性。在这里，我们报告了一种无偏、多步骤的 ADP-核糖组数据分析工作流程的建立，该工作流程导致鉴定酪氨酸为新型 ARTD1/PARP1 依赖性 ADPr 接受氨基酸。对 ADP-核糖化蛋白的 MS 分析证实了酪氨酸是 RPS3A（Y155）和 HPF1（Y238）中的 ADPr 接受氨基酸，并表明 RPS3A 的 -修饰依赖于 HPF1。我们提供了一个 ADP-核糖基化位点定位谱数据库（ADPr-LSD），其中包含 288 个高质量的 ADPr 修饰肽谱，作为正确 ADPr 位点定位的 ADPr 谱参考。
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