Mick, David U.

[["dc.bibliographiccitation.firstpage","1570"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","1580"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Bareth, Bettina"],["dc.contributor.author","Nikolov, Miroslav"],["dc.contributor.author","Lorenzi, Isotta"],["dc.contributor.author","Hildenbeutel, Markus"],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Helbig, Christin"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Ott, Martin"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.editor","Fox, Thomas D."],["dc.date.accessioned","2020-12-10T18:16:05Z"],["dc.date.available","2020-12-10T18:16:05Z"],["dc.date.issued","2016"],["dc.description.abstract","The mitochondrial cytochrome c oxidase assembles in the inner membrane from subunits of dual genetic origin. The assembly process of the enzyme is initiated by membrane insertion of the mitochondria-encoded Cox1 subunit. During complex maturation, transient assembly intermediates, consisting of structural subunits and specialized chaperone-like assembly factors, are formed. In addition, cofactors such as heme and copper have to be inserted into the nascent complex. To regulate the assembly process, the availability of Cox1 is under control of a regulatory feedback cycle in which translation of COX1 mRNA is stalled when assembly intermediates of Cox1 accumulate through inactivation of the translational activator Mss51. Here we isolate a cytochrome c oxidase assembly intermediate in preparatory scale from coa1 Delta. mutant cells, using Mss51 as bait. We demonstrate that at this stage of assembly, the complex has not yet incorporated the heme a cofactors. Using quantitative mass spectrometry, we define the protein composition of the assembly intermediate and unexpectedly identify the putative methyltransferase Oms1 as a constituent. Our analyses show that Oms1 participates in cytochrome c oxidase assembly by stabilizing newly synthesized Cox1."],["dc.identifier.doi","10.1091/mbc.E15-12-0811"],["dc.identifier.eissn","1939-4586"],["dc.identifier.gro","3141687"],["dc.identifier.isi","000376456800004"],["dc.identifier.issn","1059-1524"],["dc.identifier.pmid","27030670"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75047"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1939-4586"],["dc.relation.issn","1059-1524"],["dc.title","Oms1 associates with cytochrome c oxidase assembly intermediates to stabilize newly synthesized Cox1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4128"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","4137"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Bareth, Bettina"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Nikolov, Miroslav"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:47:07Z"],["dc.date.available","2017-09-07T11:47:07Z"],["dc.date.issued","2013"],["dc.description.abstract","Cox1, the core subunit of the cytochrome c oxidase, receives two heme a cofactors during assembly of the 13-subunit enzyme complex. However, at which step of the assembly process and how heme is inserted into Cox1 have remained an enigma. Shy1, the yeast SURF1 homolog, has been implicated in heme transfer to Cox1, whereas the heme a synthase, Cox15, catalyzes the final step of heme a synthesis. Here we performed a comprehensive analysis of cytochrome c oxidase assembly intermediates containing Shy1. Our analyses suggest that Cox15 displays a role in cytochrome c oxidase assembly, which is independent of its functions as the heme a synthase. Cox15 forms protein complexes with Shy1 and also associates with Cox1-containing complexes independently of Shy1 function. These findings indicate that Shy1 does not serve as a mobile heme carrier between the heme a synthase and maturing Cox1 but rather cooperates with Cox15 for heme transfer and insertion in early assembly intermediates of cytochrome c oxidase."],["dc.identifier.doi","10.1128/MCB.00747-13"],["dc.identifier.gro","3142276"],["dc.identifier.isi","000324912000015"],["dc.identifier.pmid","23979592"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6487"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1098-5549"],["dc.relation.issn","0270-7306"],["dc.title","The Heme a Synthase Cox15 Associates with Cytochrome c Oxidase Assembly Intermediates during Cox1 Maturation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Mick, D. U."],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Wiese, H."],["dc.contributor.author","Warscheid, B."],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2018-11-07T09:16:18Z"],["dc.date.available","2018-11-07T09:16:18Z"],["dc.date.issued","2012"],["dc.identifier.isi","000209348607091"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/27909"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Cell Biology"],["dc.publisher.place","Bethesda"],["dc.relation.issn","1939-4586"],["dc.relation.issn","1059-1524"],["dc.title","MITRAC complexes link mitochondrial protein translocation to respiratory chain assembly and translational regulation."],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1528"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","1541"],["dc.bibliographiccitation.volume","151"],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Wiese, Heike"],["dc.contributor.author","Reinhold, Robert"],["dc.contributor.author","Pacheu-Grau, David"],["dc.contributor.author","Lorenzi, Isotta"],["dc.contributor.author","Sasarman, Florin"],["dc.contributor.author","Weraarpachai, Woranontee"],["dc.contributor.author","Shoubridge, Eric A."],["dc.contributor.author","Warscheid, Bettina"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:48:20Z"],["dc.date.available","2017-09-07T11:48:20Z"],["dc.date.issued","2012"],["dc.description.abstract","Mitochondrial respiratory-chain complexes assemble from subunits of dual genetic origin assisted by specialized assembly factors. Whereas core subunits are translated on mitochondrial ribosomes, others are imported after cytosolic translation. How imported subunits are ushered to assembly intermediates containing mitochondria-encoded subunits is unresolved. Here, we report a comprehensive dissection of early cytochrome c oxidase assembly intermediates containing proteins required for normal mitochondrial translation and reveal assembly factors promoting biogenesis of human respiratory-chain complexes. We find that TIM21, a subunit of the inner-membrane presequence translocase, is also present in the major assembly intermediates containing newly mitochondria-synthesized and imported respiratory-chain subunits, which we term MITRAC complexes. Human TIM21 is dispensable for protein import but required for integration of early-assembling, presequence-containing subunits into respiratory-chain intermediates. We establish an unexpected molecular link between the TIM23 transport machinery and assembly of respiratory-chain complexes that regulate mitochondrial protein synthesis in response to their assembly state."],["dc.identifier.doi","10.1016/j.cell.2012.11.053"],["dc.identifier.gro","3142426"],["dc.identifier.isi","000312890300017"],["dc.identifier.pmid","23260140"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8152"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0092-8674"],["dc.title","MITRAC Links Mitochondrial Protein Translocation to Respiratory-Chain Assembly and Translational Regulation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]