Neumann, Heinz

[["dc.bibliographiccitation.journal","FEBS Journal"],["dc.bibliographiccitation.volume","282"],["dc.contributor.author","Hoffmann, C."],["dc.contributor.author","Neumann, H."],["dc.date.accessioned","2018-11-07T09:54:50Z"],["dc.date.available","2018-11-07T09:54:50Z"],["dc.date.issued","2015"],["dc.format.extent","70"],["dc.identifier.isi","000362570601051"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36619"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.conference","40th Congress of the Federation-of-European-Biochemical-Societies (FEBS) The Biochemical Basis of Life"],["dc.relation.eventlocation","Berlin, GERMANY"],["dc.relation.issn","1742-4658"],["dc.relation.issn","1742-464X"],["dc.title","In vivo structural mapping of FACT-histone interactions using genetically encoded crosslinkers"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3495"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Cell Cycle"],["dc.bibliographiccitation.lastpage","3504"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Kari, Vijayalakshmi"],["dc.contributor.author","Shchebet, Andrei"],["dc.contributor.author","Neumann, Heinz"],["dc.contributor.author","Johnsen, Steven A."],["dc.date.accessioned","2018-11-07T08:50:42Z"],["dc.date.available","2018-11-07T08:50:42Z"],["dc.date.issued","2011"],["dc.description.abstract","Many anticancer therapies function largely by inducing DNA double-strand breaks (DSBs) or altering the ability of cancer cells to repair them. Proper and timely DNA repair requires dynamic changes in chromatin assembly and disassembly characterized by histone H3 lysine 56 acetylation (H3K56ac) and phosphorylation of the variant histone H2AX (gamma H2AX). Similarly, histone H2B monoubiquitination (H2Bub1) functions in DNA repair, but its role in controlling dynamic changes in chromatin structure following DSBs and the histone chaperone complexes involved remain unknown. Therefore, we investigated the role of the H2B ubiquitin ligase RNF40 in the DSB response. We show that RNF40 depletion results in sustained H2AX phosphorylation and a decrease in rapid cell cycle checkpoint activation. Furthermore, RNF40 knockdown resulted in decreased H3K56ac and decreased recruitment of the facilitates chromatin transcription (FACT) complex to chromatin following DSB. Knockdown of the FACT component suppressor of Ty homolog-16 (SUPT16H) phenocopied the effects of RNF40 knockdown on both gamma H2AX and H3K56ac following DSB induction. Consistently, both RNF40 and SUPT16H were required for proper DNA end resection and timely DNA repair, suggesting that H2Bub1 and FACT cooperate to increase chromatin dynamics, which facilitates proper checkpoint activation and timely DNA repair. These results provide important mechanistic insights into the tumor suppressor function of H2Bub1 and provide a rational basis for pursuing H2Bub1-based therapies in conjunction with traditional chemo-and radiotherapy."],["dc.identifier.doi","10.4161/cc.10.20.17769"],["dc.identifier.isi","000296570700027"],["dc.identifier.pmid","22031019"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21752"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Landes Bioscience"],["dc.relation.issn","1538-4101"],["dc.title","The H2B ubiquitin ligase RNF40 cooperates with SUPT16H to induce dynamic changes in chromatin structure during DNA double-strand break repair"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["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.firstpage","2817"],["dc.bibliographiccitation.issue","14"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","2828"],["dc.bibliographiccitation.volume","129"],["dc.contributor.author","Desfougeres, Yann"],["dc.contributor.author","Neumann, Heinz"],["dc.contributor.author","Mayer, Andreas"],["dc.date.accessioned","2018-11-07T10:11:33Z"],["dc.date.available","2018-11-07T10:11:33Z"],["dc.date.issued","2016"],["dc.description.abstract","Cells control the size of their compartments relative to cell volume, but there is also size control within each organelle. Yeast vacuoles neither burst nor do they collapse into a ruffled morphology, indicating that the volume of the organellar envelope is adjusted to the amount of content. It is poorly understood how this adjustment is achieved. We show that the accumulating content of yeast vacuoles activates fusion of other vacuoles, thus increasing the volume-to-surface ratio. Synthesis of the dominant compound stored inside vacuoles, polyphosphate, stimulates binding of the chaperone Sec18/NSF to vacuolar SNAREs, which activates them and triggers fusion. SNAREs can only be activated by lumenal, not cytosolic, polyphosphate (polyP). Control of lumenal polyP over SNARE activation in the cytosol requires the cytosolic cyclin-dependent kinase Pho80-Pho85 and the R-SNARE Nyv1. These results suggest that cells can adapt the volume of vacuoles to their content through feedback from the vacuole lumen to the SNAREs on the cytosolic surface of the organelle."],["dc.identifier.doi","10.1242/jcs.184382"],["dc.identifier.isi","000380928600014"],["dc.identifier.pmid","27252384"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40073"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Company Of Biologists Ltd"],["dc.relation.issn","1477-9137"],["dc.relation.issn","0021-9533"],["dc.title","Organelle size control - increasing vacuole content activates SNAREs to augment organelle volume through homotypic fusion"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","73"],["dc.bibliographiccitation.journal","Glia"],["dc.bibliographiccitation.lastpage","74"],["dc.contributor.author","Liu, Y."],["dc.contributor.author","Heine, H."],["dc.contributor.author","Neumann, H."],["dc.contributor.author","Fassbender, Klaus"],["dc.date.accessioned","2018-11-07T10:36:32Z"],["dc.date.available","2018-11-07T10:36:32Z"],["dc.date.issued","2003"],["dc.identifier.isi","000184938300320"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/45349"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-liss"],["dc.publisher.place","New york"],["dc.relation.conference","6th European Meeting on Glial Cell Function in Health and Disease"],["dc.relation.eventlocation","BERLIN, GERMANY"],["dc.relation.issn","0894-1491"],["dc.title","Cd14-dependent phagocytosis of Alzheimer's amyloid beta-peptide"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["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.firstpage","453"],["dc.bibliographiccitation.journal","Metabolic Engineering"],["dc.bibliographiccitation.lastpage","462"],["dc.bibliographiccitation.volume","47"],["dc.contributor.author","Heitmüller, Svenja"],["dc.contributor.author","Neumann-Staubitz, Petra"],["dc.contributor.author","Herrfurth, Cornelia"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Neumann, Heinz"],["dc.date.accessioned","2020-12-10T15:21:49Z"],["dc.date.available","2020-12-10T15:21:49Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1016/j.ymben.2018.04.022"],["dc.identifier.issn","1096-7176"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73173"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Cellular substrate limitations of lysine acetylation turnover by sirtuins investigated with engineered futile cycle enzymes"],["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"]]