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TitleOpposing roles of H3- and H4-acetylation in the regulation of nucleosome structure––a FRET study.
Publication TypeJournal Article
Year of Publication2015
AuthorsGansen, Alexander, Katalin Toth, Nathalie Schwarz, and Jörg Langowski
JournalNucleic Acids Res
Volume43
Issue3
Pagination1433-43
Date Published2015 Feb 18
ISSN1362-4962
Abstract

Using FRET in bulk and on single molecules, we assessed the structural role of histone acetylation in nucleosomes reconstituted on the 170 bp long Widom 601 sequence. We followed salt-induced nucleosome disassembly, using donor–acceptor pairs on the ends or in the internal part of the nucleosomal DNA, and on H2B histone for measuring H2A/H2B dimer exchange. This allowed us to distinguish the influence of acetylation on salt-induced DNA unwrapping at the entry–exit site from its effect on nucleosome core dissociation. The effect of lysine acetylation is not simply cumulative, but showed distinct histone-specificity. Both H3- and H4-acetylation enhance DNA unwrapping above physiological ionic strength; however, while H3-acetylation renders the nucleosome core more sensitive to salt-induced dissociation and to dimer exchange, H4-acetylation counteracts these effects. Thus, our data suggest, that H3- and H4-acetylation have partially opposing roles in regulating nucleosome architecture and that distinct aspects of nucleosome dynamics might be independently controlled by individual histones.

DOI10.1093/nar/gku1354
Alternate JournalNucleic Acids Res.
PubMed ID25589544
PubMed Central IDPMC4330349