Stoldt, Stefan

[["dc.bibliographiccitation.firstpage","2292"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","2301"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Stoldt, Stefan"],["dc.contributor.author","Wenzel, Dirk"],["dc.contributor.author","Hildenbeutel, Markus"],["dc.contributor.author","Wurm, Christian Andreas"],["dc.contributor.author","Herrmann, Johannes M."],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2017-09-07T11:48:51Z"],["dc.date.available","2017-09-07T11:48:51Z"],["dc.date.issued","2012"],["dc.description.abstract","The Oxa1 protein is a well-conserved integral protein of the inner membrane of mitochondria. It mediates the insertion of both mitochondrial-and nuclear-encoded proteins from the matrix into the inner membrane. We investigated the distribution of budding yeast Oxa1 between the two subdomains of the contiguous inner membrane-the cristae membrane (CM) and the inner boundary membrane (IBM)-under different physiological conditions. We found that under fermentable growth conditions, Oxa1 is enriched in the IBM, whereas under nonfermentable (respiratory) growth conditions, it is predominantly localized in the CM. The enrichment of Oxa1 in the CM requires mitochondrial translation; similarly, deletion of the ribosome-binding domain of Oxa1 prevents an enrichment of Oxa1 in the CM. The predominant localization in the IBM under fermentable growth conditions is prevented by inhibiting mitochondrial protein import. Furthermore, overexpression of the nuclear-encoded Oxa1 substrate Mdl1 shifts the distribution of Oxa1 toward the IBM. Apparently, the availability of nuclear- and mitochondrial-encoded substrates influences the inner-membrane distribution of Oxa1. Our findings show that the distribution of Oxa1 within the inner membrane is dynamic and adapts to different physiological needs."],["dc.identifier.doi","10.1091/mbc.E11-06-0538"],["dc.identifier.gro","3142518"],["dc.identifier.isi","000306286700006"],["dc.identifier.pmid","22513091"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9497"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8878"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1059-1524"],["dc.rights","CC BY-NC-SA 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-sa/3.0"],["dc.title","The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2412"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","2421"],["dc.bibliographiccitation.volume","117"],["dc.contributor.author","Toth, Alexandra"],["dc.contributor.author","Meyrat, Axel"],["dc.contributor.author","Stoldt, Stefan"],["dc.contributor.author","Santiago, Ricardo"],["dc.contributor.author","Wenzel, Dirk"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","von Ballmoos, Christoph"],["dc.contributor.author","Ott, Martin"],["dc.date.accessioned","2020-12-10T18:12:55Z"],["dc.date.available","2020-12-10T18:12:55Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1073/pnas.1917968117"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74534"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/42"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | A05: Mitochondriale Heterogenität in Synapsen"],["dc.relation.workinggroup","RG Jakobs (Structure and Dynamics of Mitochondria)"],["dc.title","Kinetic coupling of the respiratory chain with ATP synthase, but not proton gradients, drives ATP production in cristae membranes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","541"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Biology of the Cell"],["dc.bibliographiccitation.lastpage","552"],["dc.bibliographiccitation.volume","99"],["dc.contributor.author","Stoldt, Stefan"],["dc.contributor.author","Wenzel, Dirk"],["dc.contributor.author","Schulze, Ekkehard"],["dc.contributor.author","Doenecke, Detlef"],["dc.contributor.author","Happel, Nicole"],["dc.date.accessioned","2018-11-07T10:57:56Z"],["dc.date.available","2018-11-07T10:57:56Z"],["dc.date.issued","2007"],["dc.description.abstract","Background information: H1 histones are a protein family comprising several subtypes. Although specific functions of the individual subtypes could not be determined so far, differential roles are indicated by varied nuclear distributions as well as differential expression patterns of the H1 subtypes. Although the group of replication-dependent H1 subtypes is synthesized during S phase, the replacement H1 subtype, H1 degrees, is also expressed in a replication-independent manner in non-proliferating cells. Recently we showed, by protein biochemical analysis, that the ubiquitously expressed subtype H1x is enriched in the micrococcal nuclease-resistant part of chromatin and that, although it shares common features with H1 degrees, its expression is differentially regulated, since, in contrast to H1 0, growth arrest or induction of differentiation did not induce an accumulation of H1x. Results: In the present study, we show that H1 x exhibits a cell-cycle-dependent change of its nuclear distribution. This H1 subtype showed a nucleolar accumulation during the G(1) phase, and it was evenly distributed in the nucleus during S phase and G(2). Immunocytochemical analysis of the intranucleolar distribution of H1x indicated that it is located mainly in the condensed nucleolar chromatin. In addition, we demonstrate that the amount of H1x protein remained nearly unchanged during S phase progression, which is in contrast to the replication-dependent subtypes. Conclusion: These results suggest that the differential localization of H1x provides a mechanism for a control of H1x activity by means of shuttling between nuclear subcompartments instead of a controlled turnover of the protein."],["dc.identifier.doi","10.1042/BC20060117"],["dc.identifier.isi","000250361300001"],["dc.identifier.pmid","17868027"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/50368"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Portland Press Ltd"],["dc.relation.issn","0248-4900"],["dc.title","G(1) phase-dependent nucleolar accumulation of human histone H1x"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","528"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Nature Cell Biology"],["dc.bibliographiccitation.lastpage","534"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Stoldt, Stefan"],["dc.contributor.author","Wenzel, Dirk"],["dc.contributor.author","Kehrein, Kirsten"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Ott, Martin"],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2020-12-10T18:09:54Z"],["dc.date.available","2020-12-10T18:09:54Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1038/s41556-018-0090-7"],["dc.identifier.pmid","29662179"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73796"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/28"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P01: Untersuchung der Unterschiede in der Zusammensetzung, Funktion und Position von individuellen MICOS Komplexen in einzelnen Säugerzellen"],["dc.relation.workinggroup","RG Jakobs (Structure and Dynamics of Mitochondria)"],["dc.title","Spatial orchestration of mitochondrial translation and OXPHOS complex assembly"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]