Premium
Identification of hydroxylation at aromatic amino acid residues in yeast kinase using mass spectrometry with affinity enrichment
Author(s) -
Zheng Shuzhen,
Bai Xue,
Tian Shanshan,
Wang Guojuan,
Zhai Guijin,
Guo Zhenchang,
Bi Wenjing,
Shen Lijin,
Zhang Kai
Publication year - 2016
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.7644
Subject(s) - chemistry , hydroxylation , mass spectrometry , yeast , chromatography , biochemistry , enzyme
Rationale Protein kinases represent the key elements in phosphorylation‐based signal transmission. Recent studies suggest that hydroxylation may mediate activities of protein kinases. This paper aims to examine the hydroxylation in protein kinases for improving our understanding of the protein modification. Methods We combined affinity‐based protein purification with MS analysis for identification of novel hydroxylation at aromatic amino acid residues in yeast kinases. Results We identified 17 hydroxylation at aromatic amino acid residues (10 at Phe, 1 at Tyr and 6 at Trp) using MS analysis. We further characterized the localization and studied the potential significance of these modifications. Conclusions This is a new report on the identification of hydroxylation at aromatic amino acid residues in yeast kinases. This study expands the catalog of hydroxylation in kinases and suggests the potential function of hydroxylation. Copyright © 2016 John Wiley & Sons, Ltd.