NMR studies on the N-terminal acetylation domain of histone H4

Histones, nuclear proteins that interact with DNA to form nucleosomes, are essential for both the regulation of transcription and the packaging of DNA within chromosomes. The N-terminal domain of histone H4 which contains fou r acetylation sites at lysines, may play a separate role in chromatin struc ture from the remainder of the H4 chain. NMR data suggest that H4(NTP) pept ide does have relating disordered structure at physiological pH, however, i t has a defined structure at lower pH conditions. The solution structure ca lculated from NMR data shows a well structured region comprising residues o f Val21-Asp24. In addition. our results suggest that the H4(NTP) prefers an extended backbone conformation at acetylation sites, however, it (especial ly Lys(12)) became more defined structures after acetylation for its optimu m function.