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

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

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
Volume269
Issue number1-2
DOIs
StatePublished - Jan 1 2008
Externally publishedYes

Fingerprint

acetylation
Acetylation
chromatin
methylation
Methylation
lysine
qualitative analysis
yeast
chickens
Histones
Yeast
quantitative analysis
Lysine
Chromatin
erythrocytes
Chemical analysis
Transcription
saccharomyces
organisms
Mass spectrometry

Keywords

  • Histone
  • Histone acetylation
  • Histone methylation
  • Mass spectrometry

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Spectroscopy

Cite this

Qualitative and quantitative analysis of lysine acetylation and methylation in yeast histone H3. / Zhang, Kangling.

In: International Journal of Mass Spectrometry, Vol. 269, No. 1-2, 01.01.2008, p. 101-111.

Research output: Contribution to journalArticle

@article{b5e5556655d8404c87a4976193c831a0,
title = "Qualitative and quantitative analysis of lysine acetylation and methylation in yeast histone H3",
abstract = "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.",
keywords = "Histone, Histone acetylation, Histone methylation, Mass spectrometry",
author = "Kangling Zhang",
year = "2008",
month = "1",
day = "1",
doi = "10.1016/j.ijms.2007.09.010",
language = "English (US)",
volume = "269",
pages = "101--111",
journal = "International Journal of Mass Spectrometry",
issn = "1387-3806",
publisher = "Elsevier",
number = "1-2",

}

TY - JOUR

T1 - Qualitative and quantitative analysis of lysine acetylation and methylation in yeast histone H3

AU - Zhang, Kangling

PY - 2008/1/1

Y1 - 2008/1/1

N2 - 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.

AB - 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.

KW - Histone

KW - Histone acetylation

KW - Histone methylation

KW - Mass spectrometry

UR - http://www.scopus.com/inward/record.url?scp=36549022132&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=36549022132&partnerID=8YFLogxK

U2 - 10.1016/j.ijms.2007.09.010

DO - 10.1016/j.ijms.2007.09.010

M3 - Article

AN - SCOPUS:36549022132

VL - 269

SP - 101

EP - 111

JO - International Journal of Mass Spectrometry

JF - International Journal of Mass Spectrometry

SN - 1387-3806

IS - 1-2

ER -