Refine your search:     
Report No.

How does an acetylation affect conformation of an H3 histone tail?

Ikebe, Kimiyoshi; Sakuraba, Shun*; Kono, Hidetoshi

In eukaryotic cells, genome DNA forms nucleosomes composed of DNA wrapped around a histone octamer: two copies of H3, H4, H2A, and H2B histone proteins, and it is compactly stored in the nucleus. The nucleosomes fold into a higher order aggregate, called as chromatin. Although the highly condensed chromatin packing disturbs access of transcriptional factors to DNA, transcription is systematically regulated in vivo. Probably, acetylation will direct dissociation of the tails from DNA, which will result in allowing DNA-binding proteins to access DNA. However, the detailed mechanism has not yet been verified because the conformational information of histone tails is difficult to obtain experimentally and is missing. To elucidate the information, we performed conformational sampling for H3 histone tails with and without acetylation. The results showed that whether acetylated or not, the tails were almost always located nearby DNA and would not dissociate from DNA contrary to the conventional view. The acetylation slightly weakens interactions between the tail and DNA and enhances the alpha-helix formation. We infer that the tail compaction caused by the alpha-helix formation induces unwrapping of DNA at entry and exit regions more and increases the chance of DNA-binding proteins bind to DNA. The results give a new view of how acetylation affects chromatin conformation.



- Accesses





[CLARIVATE ANALYTICS], [WEB OF SCIENCE], [HIGHLY CITED PAPER & CUP LOGO] and [HOT PAPER & FIRE LOGO] are trademarks of Clarivate Analytics, and/or its affiliated company or companies, and used herein by permission and/or license.