The in silico interplay between post-translational modification in histone H4 and its role in mouse spermatogenesis

The nucleosome is the fundamental repeating unit of chromatin,which consist of histone proteins h2a h2b,h3 and h4) wrapped by 147 base pairs of dna. post-translational modifications (ptms) of histones (including acetylation,phosphorylation and methylation) regulate chromatin structure and function. the combination of ptms of histone proteins regulates various cellular pathways. phosphorylated h2a and h4 are found in mouse spermatogenesis,and correlates with both mitotic/meiotic chromosome condensation and displacement of histone proteins from the nucleosome structure. another equally abundant ptm is o-glcnac modification of ser and/or thr in cytoplasmic and nuclear proteins. some ser and/or thr residues,are also available to phosphorylation (yin yang sites) in addition to o-glcnac modification,which occurs in an inverse manner. by using computational methods in silico yin yang sites in h4 are proposed,and the interplay between phosphorylation,o-glcnac modification acetylation and phosphorylation is investigated. the in silico results suggest that o-glcnac modification play a role in spermatogenesis in mammals. copyright 2010 zoological society of pakistan.