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Background: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. Histone H1.5 is an H1 isotype expressed in somatic cells and is heavily phosphorylated during mitosis. Phosphorylation of H1.5 at serine 17 appears in prometaphase and disappears in telophase. The hyperphosphorylated form of H1.5 is mainly chromatin-bound in metaphase when chromatin is maximally condensed. Phosphorylation of H1.5 at serine 17 can be catalyzed by GSK-3.
