Neumann, Heinz

[["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.firstpage","75"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Applied Microbiology and Biotechnology"],["dc.bibliographiccitation.lastpage","86"],["dc.bibliographiccitation.volume","87"],["dc.contributor.author","Neumann, Heinz"],["dc.contributor.author","Neumann-Staubitz, Petra"],["dc.date.accessioned","2018-11-07T08:42:25Z"],["dc.date.available","2018-11-07T08:42:25Z"],["dc.date.issued","2010"],["dc.description.abstract","Synthetic biology is the attempt to apply the concepts of engineering to biological systems with the aim to create organisms with new emergent properties. These organisms might have desirable novel biosynthetic capabilities, act as biosensors or help us to understand the intricacies of living systems. This approach has the potential to assist the discovery and production of pharmaceutical compounds at various stages. New sources of bioactive compounds can be created in the form of genetically encoded small molecule libraries. The recombination of individual parts has been employed to design proteins that act as biosensors, which could be used to identify and quantify molecules of interest. New biosynthetic pathways may be designed by stitching together enzymes with desired activities, and genetic code expansion can be used to introduce new functionalities into peptides and proteins to increase their chemical scope and biological stability. This review aims to give an insight into recently developed individual components and modules that might serve as parts in a synthetic biology approach to pharmaceutical biotechnology."],["dc.description.sponsorship","German Initiative of Excellence; German Research Foundation"],["dc.identifier.doi","10.1007/s00253-010-2578-3"],["dc.identifier.isi","000277784100008"],["dc.identifier.pmid","20396881"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/4236"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19695"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0175-7598"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Synthetic biology approaches in drug discovery and pharmaceutical biotechnology"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Proteomes"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Kusch, Kathrin"],["dc.contributor.author","Uecker, Marina"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Hoffmann, Christian"],["dc.contributor.author","Neumann, Heinz"],["dc.contributor.author","Werner, Hauke"],["dc.contributor.author","Jahn, Olaf"],["dc.date.accessioned","2020-12-10T18:47:19Z"],["dc.date.available","2020-12-10T18:47:19Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.3390/proteomes5010003"],["dc.identifier.eissn","2227-7382"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78723"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.publisher","MDPI"],["dc.relation.eissn","2227-7382"],["dc.rights","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Partial Immunoblotting of 2D-Gels: A Novel Method to Identify Post-Translationally Modified Proteins Exemplified for the Myelin Acetylome"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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","15"],["dc.bibliographiccitation.journal","Current Opinion in Cell Biology"],["dc.bibliographiccitation.lastpage","22"],["dc.bibliographiccitation.volume","40"],["dc.contributor.author","Antonin, Wolfram"],["dc.contributor.author","Neumann, Heinz"],["dc.date.accessioned","2018-11-07T10:13:36Z"],["dc.date.available","2018-11-07T10:13:36Z"],["dc.date.issued","2016"],["dc.description.abstract","During eukaryotic cell division, nuclear chromatin undergoes marked changes with respect to shape and degree of compaction. Although already significantly compacted during interphase, upon entry into mitosis chromatin further condenses and individualizes to discrete chromosomes that are captured and moved independently by the mitotic spindle apparatus. Once segregated by the spindle, chromatin decondenses to re-establish its interphase structure competent for DNA replication and transcription. Although cytologically described a long time ago, the underlying molecular mechanisms of mitotic chromatin condensation and decondensation are still ill-defined. Here we summarize our current knowledge of mitotic chromatin restructuring and recent progress in the field."],["dc.identifier.doi","10.1016/j.ceb.2016.01.013"],["dc.identifier.isi","000376996800004"],["dc.identifier.pmid","26895139"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13369"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40465"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1879-0410"],["dc.relation.issn","0955-0674"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","Chromosome condensation and decondensation during mitosis"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]