Wilkins, Bryan J.

[["dc.bibliographiccitation.firstpage","77"],["dc.bibliographiccitation.issue","6166"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","80"],["dc.bibliographiccitation.volume","343"],["dc.contributor.author","Wilkins, Bryan J."],["dc.contributor.author","Rall, Nils A."],["dc.contributor.author","Ostwal, Yogesh"],["dc.contributor.author","Kruitwagen, Tom"],["dc.contributor.author","Hiragami-Hamada, Kyoko"],["dc.contributor.author","Winkler, Marco"],["dc.contributor.author","Barral, Yves"],["dc.contributor.author","Fischle, Wolfgang"],["dc.contributor.author","Neumann, Heinz"],["dc.date.accessioned","2018-11-07T09:45:15Z"],["dc.date.available","2018-11-07T09:45:15Z"],["dc.date.issued","2014"],["dc.description.abstract","Metaphase chromosomes are visible hallmarks of mitosis, yet our understanding of their structure and of the forces shaping them is rudimentary. Phosphorylation of histone H3 serine 10 (H3 S10) by Aurora B kinase is a signature event of mitosis, but its function in chromatin condensation is unclear. Using genetically encoded ultraviolet light-inducible cross-linkers, we monitored protein-protein interactions with spatiotemporal resolution in living yeast to identify the molecular details of the pathway downstream of H3 S10 phosphorylation. This modification leads to the recruitment of the histone deacetylase Hst2p that subsequently removes an acetyl group from histone H4 lysine 16, freeing the H4 tail to interact with the surface of neighboring nucleosomes and promoting fiber condensation. This cascade of events provides a condensin-independent driving force of chromatin hypercondensation during mitosis."],["dc.identifier.doi","10.1126/science.1244508"],["dc.identifier.isi","000329162000051"],["dc.identifier.pmid","24385627"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34572"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Assoc Advancement Science"],["dc.relation.issn","1095-9203"],["dc.relation.issn","0036-8075"],["dc.title","A Cascade of Histone Modifications Induces Chromatin Condensation in Mitosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","11310"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Hiragami-Hamada, Kyoko"],["dc.contributor.author","Soeroes, Szabolcs"],["dc.contributor.author","Nikolov, Miroslav"],["dc.contributor.author","Wilkins, Bryan J."],["dc.contributor.author","Kreuz, Sarah"],["dc.contributor.author","Chen, Carol"],["dc.contributor.author","De La Rosa-Velazquez, Inti A."],["dc.contributor.author","Zenn, Hans Michael"],["dc.contributor.author","Kost, Nils"],["dc.contributor.author","Pohl, Wiebke"],["dc.contributor.author","Chernev, Aleksandar"],["dc.contributor.author","Schwarzer, Dirk"],["dc.contributor.author","Jenuwein, Thomas"],["dc.contributor.author","Lorincz, Matthew"],["dc.contributor.author","Zimmermann, Bastian"],["dc.contributor.author","Walla, Peter Jomo"],["dc.contributor.author","Neumann, Heinz"],["dc.contributor.author","Baubec, Tuncay"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Fischle, Wolfgang"],["dc.date.accessioned","2018-11-07T10:16:11Z"],["dc.date.available","2018-11-07T10:16:11Z"],["dc.date.issued","2016"],["dc.description.abstract","Histone H3 trimethylation of lysine 9 (H3K9me3) and proteins of the heterochromatin protein 1 (HP1) family are hallmarks of heterochromatin, a state of compacted DNA essential for genome stability and long-term transcriptional silencing. The mechanisms by which H3K9me3 and HP1 contribute to chromatin condensation have been speculative and controversial. Here we demonstrate that human HP1 beta is a prototypic HP1 protein exemplifying most basal chromatin binding and effects. These are caused by dimeric and dynamic interaction with highly enriched H3K9me3 and are modulated by various electrostatic interfaces. HP1 beta bridges condensed chromatin, which we postulate stabilizes the compacted state. In agreement, HP1 beta genome-wide localization follows H3K9me3-enrichment and artificial bridging of chromatin fibres is sufficient for maintaining cellular heterochromatic conformation. Overall, our findings define a fundamental mechanism for chromatin higher order structural changes caused by HP1 proteins, which might contribute to the plastic nature of condensed chromatin."],["dc.identifier.doi","10.1038/ncomms11310"],["dc.identifier.isi","000374291900001"],["dc.identifier.pmid","27090491"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13282"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40987"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","2041-1723"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Dynamic and flexible H3K9me3 bridging via HP1 beta dimerization establishes a plastic state of condensed chromatin"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]