Modulation of the chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of four core histone proteins (H2A, H2B, H3 and H4), is the primary building block of chromatin (1). The N-terminal tail of core histones undergoes different posttranslational modifications including acetylation, phosphorylation and methylation (2-4). These modifications occur in response to cell signal stimuli and have a direct effect on gene expression. In most species, the histone H2B is primarily acetylated at lysines 5, 12, 15 and 20 (4,5). Histone H3 is primarily acetylated at lysines 9, 14, 18 and 23 (2,3). Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms (2,3). Phosphorylation at Ser10 of histone H3 is tightly correlated with chromosome condensation during both mitosis and meiosis (6).

Purified by Protein A and peptide affinity chromatography.

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