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Influence of histone tails and H4 tail acetylations on nucleosome–nucleosome interactions

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Influence of histone tails and H4 tail acetylations on nucleosome–nucleosome interactions

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dc.contributor.author Liu, Ying
dc.contributor.author Lu, Chenning
dc.contributor.author Yang, Ye
dc.contributor.author Fan, Yanping
dc.contributor.author Yang, Renliang
dc.contributor.author Liu, Chuan Fa
dc.contributor.author Korolev, Nikolay
dc.contributor.author Nordenskiöld, Lars
dc.date.accessioned 2012-05-24T00:46:13Z
dc.date.available 2012-05-24T00:46:13Z
dc.date.copyright 2011
dc.date.issued 2012-05-24
dc.identifier.citation Liu, Y., Lu, C., Yang, Y., Fan, Y., Yang, R., Liu, C. F., et al. (2011). Influence of histone tails and H4 tail acetylations on nucleosome–nucleosome interactions. Journal of molecular biology, 414(5), 749–764.
dc.identifier.uri http://hdl.handle.net/10220/8142
dc.description.abstract Nucleosome–nucleosome interaction plays a fundamental role in chromatin folding and self-association. The cation-induced condensation of nucleosome core particles (NCPs) displays properties similar to those of chromatin fibers, with important contributions from the N-terminal histone tails. We study the self-association induced by addition of cations [Mg2+, Ca2+, cobalt(III)hexammine3+, spermidine3+ and spermine4+] for NCPs reconstituted with wild-type unmodified histones and with globular tailless histones and for NCPs with the H4 histone tail having lysine (K) acetylations or lysine-to-glutamine mutations at positions K5, K8, K12 and K16. In addition, the histone construct with the single H4K16 acetylation was investigated. Acetylated histones were prepared by a semisynthetic native chemical ligation method. The aggregation behavior of NCPs shows a general cation-dependent behavior similar to that of the self-association of nucleosome arrays. Unlike nucleosome array self-association, NCP aggregation is sensitive to position and nature of the H4 tail modification. The tetra-acetylation in the H4 tail significantly weakens the nucleosome–nucleosome interaction, while the H4 K → Q tetra-mutation displays a more modest effect. The single H4K16 acetylation also weakens the self-association of NCPs, which reflects the specific role of H4K16 in the nucleosome–nucleosome stacking. Tailless NCPs can aggregate in the presence of oligocations, which indicates that attraction also occurs by tail-independent nucleosome–nucleosome stacking and DNA–DNA attraction in the presence of cations. The experimental data were compared with the results of coarse-grained computer modeling for NCP solutions with explicit presence of mobile ions.
dc.format.extent 45 p.
dc.language.iso en
dc.relation.ispartofseries Journal of molecular biology
dc.rights © 2011 Elsevier. This is the author created version of a work that has been peer reviewed and accepted for publication by Journal of molecular biology, Elsevier. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [DOI: http://dx.doi.org/10.1016/j.jmb.2011.10.031 ]
dc.subject DRNTU::Science::Biological sciences.
dc.title Influence of histone tails and H4 tail acetylations on nucleosome–nucleosome interactions
dc.type Journal Article
dc.identifier.doi http://dx.doi.org/10.1016/j.jmb.2011.10.031
dc.identifier.rims 165585

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