Vukotic, Milena

[["dc.bibliographiccitation.firstpage","23769"],["dc.bibliographiccitation.issue","45"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","23778"],["dc.bibliographiccitation.volume","291"],["dc.contributor.author","Römpler, Katharina"],["dc.contributor.author","Müller, Tobias"],["dc.contributor.author","Juris, Lisa"],["dc.contributor.author","Wissel, Mirjam"],["dc.contributor.author","Vukotic, Milena"],["dc.contributor.author","Hofmann, Kay"],["dc.contributor.author","Deckers, Markus"],["dc.date.accessioned","2020-12-10T18:12:56Z"],["dc.date.available","2020-12-10T18:12:56Z"],["dc.date.issued","2016"],["dc.description.abstract","The mitochondrial electron transport chain consists of individual protein complexes arranged into large macromolecular structures, termed respiratory chain supercomplexes or respirasomes. In the yeast Saccharomyces cerevisiae, respiratory chain supercomplexes form by association of the bc(1) complex with the cytochrome c oxidase. Formation and maintenance of these assemblies are promoted by specific respiratory supercomplex factors, the Rcf proteins. For these proteins a regulatory function in bridging the electron transfer within supercomplexes has been proposed. Here we report on the maturation of Rcf2 into an N- and C-terminal peptide. We show that the previously uncharacterized Rcf3 (YBR255c-A) is a homolog of the N-terminal Rcf2 peptide, whereas Rcf1 is homologous to the C-terminal portion. Both Rcf3 and the C-terminal fragment of Rcf2 associate with monomeric cytochrome c oxidase and respiratory chain supercomplexes. A lack of Rcf2 and Rcf3 increases oxygen flux through the respiratory chain by up-regulation of the cytochrome c oxidase activity. A double gene deletion of RCF2 and RCF3 affects cellular survival under non-fermentable growth conditions, suggesting an overlapping role for both proteins in the regulation of the OXPHOS activity. Furthermore, our data suggest an association of all three Rcf proteins with the bc(1) complex in the absence of a functional cytochrome c oxidase and identify a supercomplex independent interaction network of the Rcf proteins."],["dc.identifier.doi","10.1074/jbc.M116.734665"],["dc.identifier.eissn","1083-351X"],["dc.identifier.isi","000387884400036"],["dc.identifier.issn","0021-9258"],["dc.identifier.pmid","27662906"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74539"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","1083-351X"],["dc.relation.issn","0021-9258"],["dc.title","Overlapping Role of Respiratory Supercomplex Factor Rcf2 and Its N-terminal Homolog Rcf3 in Saccharomyces cerevisiae"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","336"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Cell Metabolism"],["dc.bibliographiccitation.lastpage","347"],["dc.bibliographiccitation.volume","15"],["dc.contributor.author","Vukotic, Milena"],["dc.contributor.author","Oeljeklaus, Silke"],["dc.contributor.author","Wiese, Sebastian"],["dc.contributor.author","Vögtle, F. Nora"],["dc.contributor.author","Meisinger, Chris"],["dc.contributor.author","Meyer, Helmut E."],["dc.contributor.author","Zieseniss, Anke"],["dc.contributor.author","Katschinski, Doerthe M."],["dc.contributor.author","Jans, Daniel C."],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Warscheid, Bettina"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Deckers, Markus"],["dc.date.accessioned","2017-09-07T11:48:56Z"],["dc.date.available","2017-09-07T11:48:56Z"],["dc.date.issued","2012"],["dc.description.abstract","The terminal enzyme of the mitochondrial respiratory chain, cytochrome oxidase, transfers electrons to molecular oxygen, generating water. Within the inner mitochondrial membrane, cytochrome oxidase assembles into supercomplexes, together with other respiratory chain complexes, forming so-called respirasomes. Little is known about how these higher oligomeric structures are attained. Here we report on Rcf1 and Rcf2 as cytochrome oxidase subunits in S. cerevisiae. While Rcf2 is specific to yeast, Rcf1 is a conserved subunit with two human orthologs, RCF1a and RCF1b. Rcf1 is required for growth in hypoxia and complex assembly of subunits Cox13 and Rcf2, as well as for the oligomerization of a subclass of cytochrome oxidase complexes into respirasomes. Our analyses reveal that the cytochrome oxidase of mitochondria displays intrinsic heterogeneity with regard to its subunit composition and that distinct forms of respirasomes can be formed by complex variants."],["dc.identifier.doi","10.1016/j.cmet.2012.01.016"],["dc.identifier.gro","3142565"],["dc.identifier.isi","000301701400014"],["dc.identifier.pmid","22342701"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8930"],["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","1550-4131"],["dc.title","Rcf1 Mediates Cytochrome Oxidase Assembly and Respirasome Formation, Revealing Heterogeneity of the Enzyme Complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2985"],["dc.bibliographiccitation.issue","17"],["dc.bibliographiccitation.journal","FEBS Letters"],["dc.bibliographiccitation.lastpage","2992"],["dc.bibliographiccitation.volume","588"],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Balleininger, Martina"],["dc.contributor.author","Vukotic, Milena"],["dc.contributor.author","Römpler, Katharina"],["dc.contributor.author","Bareth, Bettina"],["dc.contributor.author","Juris, Lisa"],["dc.contributor.author","Dudek, Jan"],["dc.date.accessioned","2018-11-07T09:36:26Z"],["dc.date.available","2018-11-07T09:36:26Z"],["dc.date.issued","2014"],["dc.description.abstract","The mitochondrial respiratory chain is essential for the conversion of energy derived from the oxidation of metabolites into the membrane potential, which drives the synthesis of ATP. The electron transporting complexes bc(1) complex and the cytochrome c oxidase assemble into large supercomplexes, allowing efficient energy transduction. Currently, we have only limited information about what determines the structure of the supercomplex. Here, we characterize Aim24 in baker's yeast as a protein, which is integrated in the mitochondrial inner membrane and is required for the structural integrity of the supercomplex. Deletion of AIM24 strongly affects activity of the respiratory chain and induces a growth defect on non-fermentable medium. Our data indicate that Aim24 has a function in stabilizing the respiratory chain supercomplexes. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [SFB 1002]"],["dc.identifier.doi","10.1016/j.febslet.2014.06.006"],["dc.identifier.isi","000340882900032"],["dc.identifier.pmid","24928273"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32621"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/8"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","Najko"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A06: Molekulare Grundlagen mitochondrialer Kardiomyopathien"],["dc.relation.issn","1873-3468"],["dc.relation.issn","0014-5793"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.title","Aim24 stabilizes respiratory chain supercomplexes and is required for efficient respiration"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]