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","e10396"],["dc.bibliographiccitation.journal","eLife"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Kruitwagen, Tom"],["dc.contributor.author","Denoth-Lippuner, Annina"],["dc.contributor.author","Wilkins, Bryan J."],["dc.contributor.author","Neumann, Heinz"],["dc.contributor.author","Barral, Yves"],["dc.date.accessioned","2018-11-07T09:48:46Z"],["dc.date.available","2018-11-07T09:48:46Z"],["dc.date.issued","2015"],["dc.description.abstract","The segregation of eukaryotic chromosomes during mitosis requires their extensive folding into units of manageable size for the mitotic spindle. Here, we report on how phosphorylation at serine 10 of histone H3 (H3S10) contributes to this process. Using a fluorescence-based assay to study local compaction of the chromatin fiber in living yeast cells, we show that chromosome condensation entails two temporally and mechanistically distinct processes. Initially, nucleosome-nucleosome interaction triggered by H3 S10 phosphorylation and deacetylation of histone H4 promote short-range compaction of chromatin during early anaphase. Independently, condensin mediates the axial contraction of chromosome arms, a process peaking later in anaphase. Whereas defects in chromatin compaction have no observable effect on axial contraction and condensin inactivation does not affect short-range chromatin compaction, inactivation of both pathways causes synergistic defects in chromosome segregation and cell viability. Furthermore, both pathways rely at least partially on the deacetylase Hst2, suggesting that this protein helps coordinating chromatin compaction and axial contraction to properly shape mitotic chromosomes."],["dc.description.sponsorship","ETH Zurich; European Research Council"],["dc.identifier.doi","10.7554/eLife.10396"],["dc.identifier.isi","000373890000001"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13261"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35373"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elife Sciences Publications Ltd"],["dc.relation.issn","2050-084X"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Axial contraction and short-range compaction of chromatin synergistically promote mitotic chromosome condensation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["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"]]

[["dc.bibliographiccitation.firstpage","939"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","ACS Chemical Biology"],["dc.bibliographiccitation.lastpage","944"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Wilkins, Bryan J."],["dc.contributor.author","Hahn, Liljan E."],["dc.contributor.author","Heitmüller, Svenja"],["dc.contributor.author","Frauendorf, Holm"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Neumann, Heinz"],["dc.date.accessioned","2018-09-28T07:57:34Z"],["dc.date.available","2018-09-28T07:57:34Z"],["dc.date.issued","2015"],["dc.description.abstract","Post-translational modifications of proteins are important modulators of protein function. In order to identify the specific consequences of individual modifications, general methods are required for homogeneous production of modified proteins. The direct installation of modified amino acids by genetic code expansion facilitates the production of such proteins independent of the knowledge and availability of the enzymes naturally responsible for the modification. The production of recombinant histone H4 with genetically encoded modifications has proven notoriously difficult in the past. Here, we present a general strategy to produce histone H4 with acetylation, propionylation, butyrylation, and crotonylation on lysine residues. We produce homogeneous histone H4 containing up to four simultaneous acetylations to analyze the impact of the modifications on chromatin array compaction. Furthermore, we explore the ability of antibodies to discriminate between alternative lysine acylations by incorporating these modifications in recombinant histone H4."],["dc.identifier.doi","10.1021/cb501011v"],["dc.identifier.pmid","25590375"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15833"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1554-8937"],["dc.title","Genetically encoding lysine modifications on histone H4"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Protein Science"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Wilkins, Bryan J."],["dc.contributor.author","Neumann, Heinz"],["dc.date.accessioned","2018-11-07T09:07:55Z"],["dc.date.available","2018-11-07T09:07:55Z"],["dc.date.issued","2012"],["dc.format.extent","225"],["dc.identifier.isi","000307019800427"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/25906"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.conference","26th Annual Symposium of the Protein-Society"],["dc.relation.eventlocation","San Diego, CA"],["dc.relation.issn","0961-8368"],["dc.title","Synthetic Biology Approaches to Study Chromatin Structure and Dynamics"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]