Pacheu-Grau, David

[["dc.bibliographiccitation.artnumber","e32572"],["dc.bibliographiccitation.journal","eLife"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Aich, Abhishek"],["dc.contributor.author","Wang, Cong"],["dc.contributor.author","Chowdhury, Arpita"],["dc.contributor.author","Ronsör, Christin"],["dc.contributor.author","Pacheu-Grau, David"],["dc.contributor.author","Richter-Dennerlein, Ricarda"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2018-05-03T09:03:52Z"],["dc.date.accessioned","2021-10-27T13:21:07Z"],["dc.date.available","2018-05-03T09:03:52Z"],["dc.date.available","2021-10-27T13:21:07Z"],["dc.date.issued","2018"],["dc.description.abstract","Cytochrome c oxidase of the mitochondrial oxidative phosphorylation system reduces molecular oxygen with redox equivalent-derived electrons. The conserved mitochondrial-encoded COX1- and COX2-subunits are the heme- and copper-center containing core subunits that catalyze water formation. COX1 and COX2 initially follow independent biogenesis pathways creating assembly modules with subunit-specific, chaperone-like assembly factors that assist in redox centers formation. Here, we find that COX16, a protein required for cytochrome c oxidase assembly, interacts specifically with newly synthesized COX2 and its copper center-forming metallochaperones SCO1, SCO2, and COA6. The recruitment of SCO1 to the COX2-module is COX16- dependent and patient-mimicking mutations in SCO1 affect interaction with COX16. These findings implicate COX16 in CuA-site formation. Surprisingly, COX16 is also found in COX1-containing assembly intermediates and COX2 recruitment to COX1. We conclude that COX16 participates in merging the COX1 and COX2 assembly lines."],["dc.identifier.doi","10.7554/eLife.32572"],["dc.identifier.gro","3142446"],["dc.identifier.pmid","29381136"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15212"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/91995"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/200"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.notes.status","final"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A06: Molekulare Grundlagen mitochondrialer Kardiomyopathien"],["dc.relation.issn","2050-084X"],["dc.relation.orgunit","Universitätsmedizin Göttingen"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","COX16 promotes COX2 metallation and assembly during respiratory complex IV biogenesis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","823"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Cell Metabolism"],["dc.bibliographiccitation.lastpage","833"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Pacheu-Grau, David"],["dc.contributor.author","Bareth, Bettina"],["dc.contributor.author","Dudek, Jan"],["dc.contributor.author","Juris, Lisa"],["dc.contributor.author","Vögtle, F. Nora"],["dc.contributor.author","Wissel, Mirjam"],["dc.contributor.author","Leary, Scot C."],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Deckers, Markus"],["dc.date.accessioned","2017-09-07T11:43:47Z"],["dc.date.available","2017-09-07T11:43:47Z"],["dc.date.issued","2015"],["dc.description.abstract","Three mitochondria-encoded subunits form the catalytic core of cytochrome c oxidase, the terminal enzyme of the respiratory chain. COX1 and COX2 contain heme and copper redox centers, which are integrated during assembly of the enzyme. Defects in this process lead to an enzyme deficiency and manifest as mitochondrial disorders in humans. Here we demonstrate that COA6 is specifically required for COX2 biogenesis. Absence of COA6 leads to fast turnover of newly synthesized COX2 and a concomitant reduction in cytochrome c oxidase levels. COA6 interacts transiently with the copper-containing catalytic domain of newly synthesized COX2. Interestingly, similar to the copper metallochaperone SCO2, loss of COA6 causes cardiomyopathy in humans. We show that COA6 and SCO2 interact and that corresponding pathogenic mutations in each protein affect complex formation. Our analyses define COA6 as a constituent of the mitochondrial copper relay system, linking defects in COX2 metallation to cardiac cytochrome c oxidase deficiency."],["dc.identifier.doi","10.1016/j.cmet.2015.04.012"],["dc.identifier.gro","3141890"],["dc.identifier.isi","000355673700007"],["dc.identifier.pmid","25959673"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2211"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/131"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A06: Molekulare Grundlagen mitochondrialer Kardiomyopathien"],["dc.relation.eissn","1932-7420"],["dc.relation.issn","1550-4131"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.title","Cooperation between COA6 and SCO2 in COX2 Maturation during Cytochrome c Oxidase Assembly Links Two Mitochondrial Cardiomyopathies"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["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"]]