Unrestrictive identification of non-phosphorylation PTMs in yeast kinases by MS and PTMap

Kai Zhang, Yue Chen, Zhihong Zhang, Shengce Tao, Heng Zhu, Yingming Zhao

Research output: Contribution to journalArticlepeer-review

Abstract

A few protein PTMs, such as phosphorylation and ubiquitination, are known to be critical in regulation of protein kinase activities. However, the roles of other PTMs have not been extensively studied in kinases. Development of a comprehensive description of all types of PTMs and discovering novel in vivo PTMs in low abundance represent major analytical challenges. Toward this goal, we have developed a strategy for systematic and accurate identification of the full-spectrum of PTMs in yeast protein kinases. Our strategy involves isolation of GST-fused kinase proteins, MS analysis, and unrestrictive PTM identification by PTMap algorithm. Among the 30 purified yeast kinases, we identified 27 different types of PTMs, and 53 PTM sites, among which are 13 novel mass shifts that have not been previously reported, likely representing novel PTMs. These results represent a significant expansion of our current understanding of PTMs in kinases and suggest highly complex regulation of kinase function.

Original languageEnglish (US)
Pages (from-to)896-903
Number of pages8
JournalProteomics
Volume10
Issue number5
DOIs
StatePublished - Mar 2010

Keywords

  • Cell biology
  • Kinase
  • MS
  • PTMap
  • Protein post-translational modifications

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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