Histone H1 Sub-types in Mouse: Interplay Between Phosphorylation and O-Glycosylation

Linker histone H1 belongs to the family of proteins that are involved in organizing eukaryotic DNA into a compact structure. Many types of linker histone H1 are found in mammals; and the subtypes are cell specific and their amount in different types of cells varies according to the cell functions. Post-translational modifications occur on different amino acids in each subtype of linker histone H1 that induce conformational changes and consequently allow linker histone H1 to interact with chromatin at different stages during the cell cycle. This results in the regulation of transcription and gene expression. In this study it is proposed that O-glycosylation of linker histone H1 promotes condensation of chromatin, while, as it is known, phosphorylation of linker histone H1 activates transcription and gene regulation by decondensation of chromatin. Interplay between phosphorylation and O-βGlcNAc modification on Ser and Thr residues in each subtype of linker histone H1 during the cell cycle may result in diverse functional regulation of proteins. This in silico study describes the potential phosphorylation, glycosylation and their possible interplay sites on conserved Ser/Thr residues in various subtypes of linker histone H1 in Mus musculus.