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 four acetylation sites at lysines, may play a separate role in chromatin struc...

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Published in:Bulletin of the Korean Chemical Society 2001, Vol.22 (5), p.507-513
Main Authors: 방은정, 이창훈, 윤종복, 청주희, 이대윤, 이원태, Bang, Eun Jeong, Lee, Chang Hun, Yun, Jong Bok, Cheong, Ju Hui, Lee, Dae Yun, Lee, Won Tae
Format: Article
Language:Korean
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Summary: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 four acetylation sites at lysines, may play a separate role in chromatin structure from the remainder of the H4 chain. NMR data suggest that H4NTP peptide does have relating disordered structure at physiological pH, however, it has a defined structure at lower pH conditions. The solution structure calculated from NMR data shows a well structured region comprising residues of Val21-Asp24. In addition, our results suggest that the H4NTP prefers an extended backbone conformation at acetylation sites, however, it (especially Lys 12 ) became more defined structures after acetylation for its optimum function.
ISSN:0253-2964
1229-5949