Wissel, Mirjam

[["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.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"]]

[["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"]]

[["dc.bibliographiccitation.firstpage","2379"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Human Molecular Genetics"],["dc.bibliographiccitation.lastpage","2393"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Reinhold, Robert"],["dc.contributor.author","Bareth, Bettina"],["dc.contributor.author","Balleininger, Martina"],["dc.contributor.author","Wissel, Mirjam"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Mick, David U."],["dc.date.accessioned","2017-09-07T11:44:14Z"],["dc.date.available","2017-09-07T11:44:14Z"],["dc.date.issued","2011"],["dc.description.abstract","Defects in mitochondrial energy metabolism lead to severe human disorders, mainly affecting tissues especially dependent on oxidative phosphorylation, such as muscle and brain. Leigh Syndrome describes a severe encephalomyopathy in infancy, frequently caused by mutations in SURF1. SURF1, termed Shy1 in Saccharomyces cerevisiae, is a conserved assembly factor for the terminal enzyme of the respiratory chain, cytochrome c oxidase. Although the molecular function of SURF1/Shy1 is still enigmatic, loss of function leads to cytochrome c oxidase deficiency and reduced expression of the central subunit Cox1 in yeast. Here, we provide insights into the molecular mechanisms leading to disease through missense mutations in codons of the most conserved amino acids in SURF1. Mutations affecting G(124) do not compromise import of the SURF1 precursor protein but lead to fast turnover of the mature protein within the mitochondria. Interestingly, an (YD)-D-274 exchange neither affects stability nor localization of the protein. Instead, SURF1(Y274D) accumulates in a 200 kDa cytochrome c oxidase assembly intermediate. Using yeast as a model, we demonstrate that the corresponding Shy1(Y344D) is able to overcome the stage where cytochrome c oxidase assembly links to the feedback regulation of mitochondrial Cox1 expression. However, Shy1(Y344D) impairs the assembly at later steps, most apparent at low temperature and exhibits a dominant-negative phenotype upon overexpression. Thus, exchanging the conserved tyrosine (Y-344) with aspartate in yeast uncouples translational regulation of Cox1 from cytochrome c oxidase assembly and provides evidence for the dual functionality of Shy1."],["dc.identifier.doi","10.1093/hmg/ddr145"],["dc.identifier.gro","3142715"],["dc.identifier.isi","000290849200008"],["dc.identifier.pmid","21470975"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/150"],["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","1460-2083"],["dc.relation.issn","0964-6906"],["dc.title","Mimicking a SURF1 allele reveals uncoupling of cytochrome c oxidase assembly from translational regulation in yeast"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["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"]]