Neumann, Heinz

[["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"]]