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Background:Histone H2B is one of the core components of the nucleosome. The nucleosome is the smallest subunit of chromatin and consists of 147 base pairs of DNA wrapped around an octamer of core histone proteins (two each of Histone H2A, Histone H2B, Histone H3 and Histone H4). Histone H1 is a linker histone, present at the interface between the nucleosome core and DNA entry/exit points; it is responsible for establishing higher-order chromatin structure. Chromatin is subject to a variety of chemical modifications, including post-translational modifications of the histone proteins and the methylation of cytosine residues in the DNA. Reported histone modifications include acetylation, methylation, phosphorylation, ubiquitylation, glycosylation, ADP-ribosylation, carbonylation and SUMOylation; they play a major role in regulating gene expression. Lysine N-ε-acetylation is a dynamic, reversible and tightly regulated protein and histone modification that plays a major role in chromatin remodeling and in the regulation of gene expression in various cellular functions. Histone H2A and Histone H2B are acetylated in bulk chromatin by p300 and form acetylated Histone H2A/Histone H2B heterodimers. When DNA associates with intact core histone octamers that contain acetylated H2A/H2B dimers, the inhibition of transcriptional initiation significantly decreases, indicating that acetylation of their lysine residues may mediate transcription.
