Dennerlein, Sven

[["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","68"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Immunity"],["dc.bibliographiccitation.lastpage","83.e6"],["dc.bibliographiccitation.volume","54"],["dc.contributor.author","Almeida, Luís"],["dc.contributor.author","Dhillon-LaBrooy, Ayesha"],["dc.contributor.author","Castro, Carla N."],["dc.contributor.author","Adossa, Nigatu"],["dc.contributor.author","Carriche, Guilhermina M."],["dc.contributor.author","Guderian, Melanie"],["dc.contributor.author","Lippens, Saskia"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Hesse, Christina"],["dc.contributor.author","Lambrecht, Bart N."],["dc.contributor.author","Berod, Luciana"],["dc.contributor.author","Schauser, Leif"],["dc.contributor.author","Blazar, Bruce R."],["dc.contributor.author","Kalesse, Markus"],["dc.contributor.author","Müller, Rolf"],["dc.contributor.author","Moita, Luís F."],["dc.contributor.author","Sparwasser, Tim"],["dc.date.accessioned","2021-04-14T08:30:29Z"],["dc.date.available","2021-04-14T08:30:29Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1016/j.immuni.2020.11.001"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83254"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.issn","1074-7613"],["dc.title","Ribosome-Targeting Antibiotics Impair T Cell Effector Function and Ameliorate Autoimmunity by Blocking Mitochondrial Protein Synthesis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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.firstpage","712"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Trends in Cell Biology"],["dc.bibliographiccitation.lastpage","721"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Wang, Cong"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2018-01-18T11:02:55Z"],["dc.date.available","2018-01-18T11:02:55Z"],["dc.date.issued","2017"],["dc.description.abstract","Mitochondria maintained a genome during evolution to synthesize core subunits of the oxidative phosphorylation system. Expression of the mitochondrial genome requires intraorganellar replication, transcription, and translation. Membrane-associated ribosomes translate mitochondrial-encoded proteins and facilitate co-translational insertion of newly synthesized polypeptides into the inner membrane. Considering that mitochondrial-encoded proteins assemble with imported, nuclear-encoded proteins into enzyme complexes of the oxidative phosphorylation system, it is expected that expression of mitochondrial genes should adapt to the availability of their nuclear-encoded partners. Recent work shows that mitochondrial translation is influenced by the cellular environment. We discuss how mitochondrial translation is affected by the cellular environment and propose models of translational plasticity that modulate mitochondrial translation in response to the availability of imported proteins."],["dc.identifier.doi","10.1016/j.tcb.2017.05.004"],["dc.identifier.pmid","28606446"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11744"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1879-3088"],["dc.subject","OXPHOS assembly; mitochondria; mitochondrial ribosome; respiratory chain; translation regulation"],["dc.title","Plasticity of Mitochondrial Translation"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["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.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Nadler, Franziska"],["dc.contributor.author","Lavdovskaia, Elena"],["dc.contributor.author","Krempler, Angelique"],["dc.contributor.author","Cruz-Zaragoza, Luis Daniel"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Richter-Dennerlein, Ricarda"],["dc.date.accessioned","2022-12-01T08:30:49Z"],["dc.date.available","2022-12-01T08:30:49Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract\r\n Translation termination requires release factors that read a STOP codon in the decoding center and subsequently facilitate the hydrolysis of the nascent peptide chain from the peptidyl tRNA within the ribosome. In human mitochondria eleven open reading frames terminate in the standard UAA or UAG STOP codon, which can be recognized by mtRF1a, the proposed major mitochondrial release factor. However, two transcripts encoding for COX1 and ND6 terminate in the non-conventional AGA or AGG codon, respectively. How translation termination is achieved in these two cases is not known. We address this long-standing open question by showing that the non-canonical release factor mtRF1 is a specialized release factor that triggers COX1 translation termination, while mtRF1a terminates the majority of other mitochondrial translation events including the non-canonical ND6. Loss of mtRF1 leads to isolated COX deficiency and activates the mitochondrial ribosome-associated quality control accompanied by the degradation of COX1 mRNA to prevent an overload of the ribosome rescue system. Taken together, these results establish the role of mtRF1 in mitochondrial translation, which had been a mystery for decades, and lead to a comprehensive picture of translation termination in human mitochondria."],["dc.identifier.doi","10.1038/s41467-022-34088-w"],["dc.identifier.pii","34088"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/117991"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-621"],["dc.relation.eissn","2041-1723"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Human mtRF1 terminates COX1 translation and its ablation induces mitochondrial ribosome-associated quality control"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","148721"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta. Bioenergetics"],["dc.bibliographiccitation.volume","1863"],["dc.contributor.author","Shumanska, Magdalena"],["dc.contributor.author","Lodygin, Dmitri"],["dc.contributor.author","Krause, Lena"],["dc.contributor.author","Ickes, Christian"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Flügel, Alexander"],["dc.contributor.author","Bogeski, Ivan"],["dc.date.accessioned","2022-10-04T10:21:17Z"],["dc.date.available","2022-10-04T10:21:17Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1016/j.bbabio.2022.148721"],["dc.identifier.pii","S0005272822001918"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/114368"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-600"],["dc.relation.issn","0005-2728"],["dc.rights.uri","https://www.elsevier.com/tdm/userlicense/1.0/"],["dc.title","Differentiation-Induced Rearrangement of the Mitochondrial Calcium Uniporter Complex Regulates T-Cell-Mediated Immunity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1004"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Circulation Research"],["dc.bibliographiccitation.lastpage","1016"],["dc.bibliographiccitation.volume","119"],["dc.contributor.author","Swain, Lija"],["dc.contributor.author","Kesemeyer, Andrea"],["dc.contributor.author","Meyer-Roxlau, Stefanie"],["dc.contributor.author","Vettel, Christiane"],["dc.contributor.author","Zieseniss, Anke"],["dc.contributor.author","Güntsch, Annemarie"],["dc.contributor.author","Jatho, Aline"],["dc.contributor.author","Becker, Andreas"],["dc.contributor.author","Nanadikar, Maithily S."],["dc.contributor.author","Morgan, Bruce"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Shah, Ajay M."],["dc.contributor.author","El-Armouche, Ali"],["dc.contributor.author","Nikolaev, Viacheslav O."],["dc.contributor.author","Katschinski, Dörthe M."],["dc.date.accessioned","2020-12-10T18:37:59Z"],["dc.date.available","2020-12-10T18:37:59Z"],["dc.date.issued","2016"],["dc.description.abstract","Rationale: Changes in redox potentials of cardiac myocytes are linked to several cardiovascular diseases. Redox alterations are currently mostly described qualitatively using chemical sensors, which however do not allow quantifying redox potentials, lack specificity, and the possibility to analyze subcellular domains. Recent advances to quantitatively describe defined redox changes include the application of genetically encoded redox biosensors. Objective: Establishment of mouse models, which allow the quantification of the glutathione redox potential (E-GSH) in the cytoplasm and the mitochondrial matrix of isolated cardiac myocytes and in Langendorff-perfused hearts based on the use of the redox-sensitive green fluorescent protein 2, coupled to the glutaredoxin 1 (Grx1-roGFP2). Methods and Results: We generated transgenic mice with cardiac myocyte-restricted expression of Grx1-roGFP2 targeted either to the mitochondrial matrix or to the cytoplasm. The response of the roGFP2 toward H2O2, diamide, and dithiothreitol was titrated and used to determine the E-GSH in isolated cardiac myocytes and in Langendorff-perfused hearts. Distinct E-GSH were observed in the cytoplasm and the mitochondrial matrix. Stimulation of the cardiac myocytes with isoprenaline, angiotensin II, or exposure to hypoxia/reoxygenation additionally underscored that these compartments responded independently. A compartment-specific response was also observed 3 to 14 days after myocardial infarction. Conclusions: We introduce redox biosensor mice as a new tool, which allows quantification of defined alterations of E-GSH in the cytoplasm and the mitochondrial matrix in cardiac myocytes and can be exploited to answer questions in basic and translational cardiovascular research."],["dc.identifier.doi","10.1161/CIRCRESAHA.116.309551"],["dc.identifier.eissn","1524-4571"],["dc.identifier.isi","000386313900013"],["dc.identifier.issn","0009-7330"],["dc.identifier.pmid","27553648"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77158"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Lippincott Williams & Wilkins"],["dc.relation.issn","1524-4571"],["dc.relation.issn","0009-7330"],["dc.title","Redox Imaging Using Cardiac Myocyte-Specific Transgenic Biosensor Mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","600"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","The FEBS Journal"],["dc.bibliographiccitation.lastpage","613"],["dc.bibliographiccitation.volume","288"],["dc.contributor.author","Kücükköse, Cansu"],["dc.contributor.author","Taskin, Asli Aras"],["dc.contributor.author","Marada, Adinarayana"],["dc.contributor.author","Brummer, Tilman"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Vögtle, Friederike‐Nora"],["dc.date.accessioned","2021-04-14T08:25:25Z"],["dc.date.available","2021-04-14T08:25:25Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1111/febs.15358"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81624"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1742-4658"],["dc.relation.issn","1742-464X"],["dc.title","Functional coupling of presequence processing and degradation in human mitochondria"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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"]]