The in Silico Interplay Between Post-Translational Modification in Histone H4 and Its Role in Mouse Spermatogenesis (Report‪)‬

Byline: Nasir-ud-Din , Afshan Kaleem, Zeeshan Iqbal and Abdul Rauf Shakoori - Emial: prof_nasir@yahoo.com Abstract.- 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.