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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.


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