MCP Danish Cancer Society
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on March 1, 2006.
This Article
Right arrow Full Text (PDF)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
M500288-MCP200v1
5/3/541    most recent
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Glossary
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bonenfant, D.
Right arrow Articles by van Oostrum, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bonenfant, D.
Right arrow Articles by van Oostrum, J.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Submitted on September 6, 2005
Revised on November 30, 2005
Accepted on November 30, 2005

Characterization of histones H2A and H2B variants and their post-translational modifications by mass spectrometry

Debora Bonenfant, Michele Coulot, Harry Towbin, Patrick Schindler, and Jan van Oostrum

Genome and Proteome Sciences, Novartis, Basel 4002

Corresponding Author: jan.van_oostrum{at}novartis.com

The nucleosome, fundamental structural unit of chromatin, contains an octamer of core histones H3, H4, H2A and H2B. Incorporation of histone variants alter the functional properties of chromatin. To understand the global dynamics of chromatin structure and function, analysis of histone variants incorporated into the nucleosome and their covalent modifications is required. Here, we report the first global mass spectrometric analysis of histone H2A and H2B variants derived from Jurkat cells. A combination of mass spectrometric techniques, HPLC separations and enzymatic digestions using endoproteinase Glu-C, endoproteinase Arg-C and trypsin have been used to identify histone H2A and H2B subtypes and their modifications. We identified nine histone H2A and eleven histone H2B subtypes, among them proteins which only had been postulated at the gene level. The two main H2A variants, H2AO and H2AC, as well as H2AL, were either acetylated at Lys 5 or phosphorylated at Ser 1. For the replacement histone H2AZ, acetylation at Lys 4 and Lys 7 was found. The main histone H2B variant, H2BA, was acetylated at Lys 12, 15 and 20. The analysis of core histone subtypes with their modifications provide a first step towards an understanding of the functional significance of the diversity of histone structures.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Nucleic Acids ResHome page
J. R. Wisniewski, A. Zougman, and M. Mann
N{varepsilon}-Formylation of lysine is a widespread post-translational modification of nuclear proteins occurring at residues involved in regulation of chromatin function
Nucleic Acids Res., February 2, 2008; 36(2): 570 - 577.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
X. Wang and J. J. Hayes
Site-specific Binding Affinities within the H2B Tail Domain Indicate Specific Effects of Lysine Acetylation
J. Biol. Chem., November 9, 2007; 282(45): 32867 - 32876.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
D. Bonenfant, H. Towbin, M. Coulot, P. Schindler, D. R. Mueller, and J. van Oostrum
Analysis of Dynamic Changes in Post-translational Modifications of Human Histones during Cell Cycle by Mass Spectrometry
Mol. Cell. Proteomics, November 1, 2007; 6(11): 1917 - 1932.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
J. R. Wisniewski, A. Zougman, S. Kruger, and M. Mann
Mass Spectrometric Mapping of Linker Histone H1 Variants Reveals Multiple Acetylations, Methylations, and Phosphorylation as Well as Differences between Cell Culture and Tissue
Mol. Cell. Proteomics, January 1, 2007; 6(1): 72 - 87.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Journal of Biological Chemistry 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.