Of all the proteins in eukaryotic cells, histones, first recognized in the late 1800s, are the proteins most frequently bound to DNA. Histones are small, highly conserved basic proteins. The interaction between histones and DNA is fundamental for the packaging of DNA around nucleosomes to form chromatin. Nucleosomes consist of a histone octamer comprised of two copies of each of the core histone proteins H2A, H2B, H3, and H4, around which approximately 147 nucleotides of DNA is wrapped. Within the nucleosome, histones H2A and H2B consist as two H2A:H2B dimers and the H3:H4 relationship is a tetramer (Kornberg and Lorch 1999). Histone H1 distinguishes itself by falling outside of the core histone group, functioning to link strands of DNA on entry and exit of the nucleosome. NH2-terminal tails of core histones extend outside of the core structure, exposing residues on these tails to dynamic posttranslational modifications (PTMs) that are critical...
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