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.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"]]