Identification and verification of lysine propionylation and butyrylation in yeast core histories using PTMap software

Kai Zhang, Yue Chen, Zhihong Zhang, Yingming Zhao

Research output: Contribution to journalArticle

97 Scopus citations

Abstract

Ten types of post-translational modifications (PTMs) known to be critical to diverse cellular functions have been described in core histone proteins. However, it remains unclear whether additional PTMs exist in histones, and if so, what roles these undiscovered signals play in epigenetic phenomena. Here, we report a systematic analysis of yeast histone PTMs by mass spectrometry in combination with protein sequence alignment using PTMap, a computer program we recently developed. We have identified, for the first time, multiple sites of lysine propionylation and butyrylation in yeast histones H2B, H3, and H4. We confirmed these modifications by Western blotting using modification-specific antibodies, MS/MS of synthetic peptides, and coelution of synthetic and in vivo-derived peptides from an HPLC column. The presence of multiple modification sites in several yeast histones suggests that these two PTMs are histone marks that are evolutionarily conserved among eukaryotes. In addition, we identified 14 novel mass shifts that do not match any known PTM, suggesting the presence of previously undescribed histone modifications. The chemical natures of these modifications remain to be determined. Our studies therefore expand current knowledge of the "histone code".

Original languageEnglish (US)
Pages (from-to)900-906
Number of pages7
JournalJournal of Proteome Research
Volume8
Issue number2
DOIs
StatePublished - Feb 2009

Keywords

  • Histones
  • Lysine butyrylation
  • Lysine propionylation
  • Protein post-translational modifications
  • Ptmap

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