Qualitative and quantitative analysis of lysine acetylation and methylation in yeast histone H3

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6 Scopus citations


Histone post-translational modifications play important roles in cell functions and the modification patterns vary significantly among different organisms. It is important that histone modification patterns be identified. Flowing our previous work-identification of acetylation and methylation sites of histone H3 in a typical transcription most inactive chromatin isolated from chicken erythrocytes, here, we report using mass spectrometry to qualitatively and quantitatively analyze histone modification pattern of H3 in a typical transcription most active chromatin isolated from Saccharomyces cerevisiae. We compared the modification patterns of histone H3 between these two functionally opposite chromatins and observed that acetylation level at K9, K14, K27, K56 and methylation level at K4 and K79 are significantly higher in S. cerevisiae than in chicken erythrocytes, methylation at K9 is higher in chicken erythrocytes than in S. cerevisiae and methylation level at K36 is unchanged in these two chromatins. Contrary to other sites, acetylation levels at K18 and K23 are higher in chicken erythrocytes than in S. cerevisiae. Our data revealed the difference of acetylation and methylation pattern of individual H3 lysine between two distinct chromatins, one with more inactive form versus the other with more active form.

Original languageEnglish (US)
Pages (from-to)101-111
Number of pages11
JournalInternational Journal of Mass Spectrometry
Issue number1-2
StatePublished - Jan 1 2008
Externally publishedYes



  • Histone
  • Histone acetylation
  • Histone methylation
  • Mass spectrometry

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Spectroscopy

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