dc.contributor.authorKorolev, Nikolay
dc.contributor.authorYu, Hang
dc.contributor.authorLyubartsev, Alexander P.
dc.contributor.authorNordenskiöld, Lars
dc.contributor.editorCase, David A.*
dc.date.accessioned2015-03-09T04:39:06Z
dc.date.available2015-03-09T04:39:06Z
dc.date.copyright2014en_US
dc.date.issued2014
dc.identifier.citationKorolev, N., Yu, H., Lyubartsev, A. P., & Nordenskiöld, L. (2014). Molecular dynamics simulations demonstrate the regulation of DNA-DNA attraction by H4 histone tail acetylations and mutations. Biopolymers, 101(10), 1051-1064.en_US
dc.identifier.issn0006-3525en_US
dc.identifier.urihttp://hdl.handle.net/10220/25198
dc.description.abstractThe positively charged N-terminal histone tails play a crucial role in chromatin compaction and are important modulators of DNA transcription, recombination, and repair. The detailed mechanism of the interaction of histone tails with DNA remains elusive. To model the unspecific interaction of histone tails with DNA, all-atom molecular dynamics (MD) simulations were carried out for systems of four DNA 22-mers in the presence of 20 or 16 short fragments of the H4 histone tail (variations of the 16-23 a. a. KRHRKVLR sequence, as well as the unmodified fragment a. a.13-20, GGAKRHRK). This setup with high DNA concentration, explicit presence of DNA-DNA contacts, presence of unstructured cationic peptides (histone tails) and K(+) mimics the conditions of eukaryotic chromatin. A detailed account of the DNA interactions with the histone tail fragments, K(+) and water is presented. Furthermore, DNA structure and dynamics and its interplay with the histone tail fragments binding are analysed. The charged side chains of the lysines and arginines play major roles in the tail-mediated DNA-DNA attraction by forming bridges and by coordinating to the phosphate groups and to the electronegative sites in the minor groove. Binding of all species to DNA is dynamic. The structure of the unmodified fully-charged H4 16-23 a.a. fragment KRHRKVLR is dominated by a stretched conformation. The H4 tail a. a. fragment GGAKRHRK as well as the H4 Lys16 acetylated fragment are highly flexible. The present work allows capturing typical features of the histone tail-counterion-DNA structure, interaction and dynamics.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesBiopolymersen_US
dc.rights© 2014 Wiley Periodicals, Inc.en_US
dc.subjectDRNTU::Science::Biological sciences
dc.titleMolecular dynamics simulations demonstrate the regulation of DNA-DNA attraction by H4 histone tail acetylations and mutationsen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.1002/bip.22499


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record