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PMID: 15598823 Published · epublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Mass spectrometry analysis of Arabidopsis histone H3 reveals distinct combinations of post-translational modifications.

Nucleic acids research ·Vol. 32 ·No. 22 ·2004-00-00 ·Pages 6511-8

Johnson L, Mollah S, Garcia BA, Muratore TL, Shabanowitz J, Hunt DF, Jacobsen SE

Abstract

Chromatin is regulated at many different levels, from higher-order packing to individual nucleosome placement. Recent studies have shown that individual histone modifications, and combinations thereof, play a key role in modulating chromatin structure and gene activity. Reported here is an analysis of Arabidopsis histone H3 modifications by nanoflow-HPLC coupled to electrospray ionization on a hybrid linear ion trap-Fourier transform mass spectrometer (LTQ/FTMS). We find that the sites of acetylation and methylation, in general, correlate well with other plants and animals. Two well-studied modifications, dimethylation of Lys-9 (correlated with silencing) and acetylation of Lys-14 (correlated with active chromatin) while abundant by themselves were rarely found on the same histone H3 tail. In contrast, dimethylation at Lys-27 and monomethylation at Lys-36 were commonly found together. Interestingly, acetylation at Lys-9 was found only in a low percentage of histones while acetylation of Lys-14 was very abundant. The two histone H3 variants, H3.1 and H3.2, also differ in the abundance of silencing and activating marks confirming other studies showing that the replication-independent histone H3 is enriched in active chromatin.

MeSH Terms
Acetylation Arabidopsis Proteins/analysis,chemistry,metabolism Blotting, Western Histones/analysis,chemistry,metabolism Methylation Protein Processing, Post-Translational Spectrometry, Mass, Electrospray Ionization
Chemicals
Arabidopsis Proteins Histones
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Johnson Lianna
Life Science Core Curriculum, Department and Molecular Biology Institute, University of California, Los Angeles, CA 90095, USA.
Mollah Sahana
Garcia Benjamin A
Muratore Tara L
Shabanowitz Jeffrey
Hunt Donald F
Jacobsen Steven E
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
1362-4962
Published
2004-00-00
Epub
2004-00-14
Pages
6511-8
Language
English
Region
England
NLM ID
0411011
PMCID
PMC545460
Subset
IM
Grants
NIGMS NIH HHS · R01 GM037537 · United States
NIGMS NIH HHS · GM37537 · United States
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