Now showing 1 - 3 of 3
  • 2016Journal Article
    [["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"]]
    Details DOI PMID PMC WOS
  • 2021Journal Article
    [["dc.bibliographiccitation.artnumber","S0167488921001877"],["dc.bibliographiccitation.firstpage","119133"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta. Molecular Cell Research"],["dc.bibliographiccitation.volume","1868"],["dc.contributor.author","Homberg, Bettina"],["dc.contributor.author","Römpler, Katharina"],["dc.contributor.author","Wissel, Mirjam"],["dc.contributor.author","Callegari, Sylvie"],["dc.contributor.author","Deckers, Markus"],["dc.date.accessioned","2021-09-01T06:42:57Z"],["dc.date.available","2021-09-01T06:42:57Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1016/j.bbamcr.2021.119133"],["dc.identifier.pii","S0167488921001877"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/89186"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-455"],["dc.relation.issn","0167-4889"],["dc.title","Rcf proteins and their differential specificity for respiratory chain complexes: A unique role for Rcf2 on oxygen sensitive supercomplexes?"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]
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  • 2016Journal Article Research Paper
    [["dc.bibliographiccitation.firstpage","1624"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],["dc.bibliographiccitation.lastpage","1632"],["dc.bibliographiccitation.volume","1863"],["dc.contributor.author","Levchenko, Maria"],["dc.contributor.author","Wuttke, Jan-Moritz"],["dc.contributor.author","Römpler, Katharina"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Neifer, Klaus"],["dc.contributor.author","Juris, Lisa"],["dc.contributor.author","Wissel, Mirjam"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Deckers, Markus"],["dc.date.accessioned","2017-09-07T11:44:49Z"],["dc.date.available","2017-09-07T11:44:49Z"],["dc.date.issued","2016"],["dc.description.abstract","The cytochrome c oxidase (COX) is the terminal enzyme of the respiratory chain. The complex accepts electrons from cytochrome c and passes them onto molecular oxygen. This process contributes to energy capture in the form of a membrane potential across the inner membrane. The enzyme complex assembles in a stepwise process from the three mitochondria-encoded core subunits Coxl, Cox2 and Cox3, which associate with nuclear-encoded subunits and cofactors. In the yeast Saccharomyces cerevisiae, the cytochrome c oxidase associates with the bc(1)-complex into supercomplexes, allowing efficient energy transduction. Here we report on Cox26 as a protein found in respiratory chain supercomplexes containing cytochrome c oxidase. Our analyses reveal Cox26 as a novel stoichiometric structural subunit of the cytochrome c oxidase. A loss of Cox26 affects cytochrome c oxidase activity and respirasome organization. (C) 2016 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.bbamcr.2016.04.007"],["dc.identifier.gro","3141656"],["dc.identifier.isi","000378360200015"],["dc.identifier.pmid","27083394"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6009"],["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","0006-3002"],["dc.relation.issn","0167-4889"],["dc.title","Cox26 is a novel stoichiometric subunit of the yeast cytochrome c oxidase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]
    Details DOI PMID PMC WOS