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Mitochondrial protein assemblies: Biogenesis of the cytochrome c oxidase and mitophagic signaling complexes

dc.contributor.advisorRehling, Peter Prof. Dr.
dc.contributor.authorLevchenko, Mariia
dc.date.accessioned2016-09-05T09:09:00Z
dc.date.available2016-09-05T09:09:00Z
dc.date.issued2016-09-05
dc.identifier.urihttp://hdl.handle.net/11858/00-1735-0000-0028-8824-B
dc.identifier.urihttp://dx.doi.org/10.53846/goediss-5841
dc.language.isoengde
dc.relation.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subject.ddc572de
dc.titleMitochondrial protein assemblies: Biogenesis of the cytochrome c oxidase and mitophagic signaling complexesde
dc.typedoctoralThesisde
dc.contributor.refereeRehling, Peter Prof. Dr.
dc.date.examination2015-12-02
dc.description.abstractengMitochondrial physiology requires a constant balance between biosynthesis and degradation events. This thesis addresses both mitochondrial biogenesis, exemplified by cytochrome c oxidase assembly, and mitochondrial removal in the course of mitophagy. The cytochrome c oxidase is the terminal enzyme of the respiratory chain. It assembles in a complicated pathway from nuclear- and mitochondria-encoded subunits. Together with other respiratory chain complexes the cytochrome c oxidase is included into supercomplexes. These oligomeric structures are implicated in efficient electron transfer and increased stability of their constituents. The first aim of this thesis was to address the role of an uncharacterized protein Cox26 in supercomplex biogenesis. I have identified Cox26 as a novel cytochrome c oxidase subunit that associates with respiratory chain supercomplexes. I discovered that Cox26 is required for efficient formation of supercomplexes and cytochrome c oxidase. Cox26 is expendable for catalytic activity of individual respiratory complexes and mitochondrial respiration. Abnormal biogenesis of the respiratory chain compromises cellular energy metabolism and leads to mitochondrial damage. Defective mitochondria have to be selectively removed in the course of mitophagy. Mitophagy receptors on mitochondrial surface provide the basis for such selectivity. Thus, the second goal of my project was to understand how yeast mitophagy receptor Atg32 governs mitochondrial recognition by the mitophagic machinery. I found that Atg32 is included into a mitochondrial complex, which dissociates during mitophagy. Atg32 is subsequently modified and delivered to the vacuole, presumably together with its cargo. Unaltered receptor is digested by an undetermined protease, possibly preventing excessive mitochondrial degradation.de
dc.contributor.coRefereeSchwappach, Blanche Prof. Dr.
dc.subject.engmitochondriade
dc.subject.engmitophagyde
dc.subject.engAtg32de
dc.subject.engCox26de
dc.subject.engmitochondrial degradationde
dc.subject.engmitochondrial quality controlde
dc.subject.engcytochrome c oxidasede
dc.subject.engsupercomplexesde
dc.subject.engrespirationde
dc.subject.engCOX assemblyde
dc.identifier.urnurn:nbn:de:gbv:7-11858/00-1735-0000-0028-8824-B-6
dc.affiliation.instituteGöttinger Graduiertenschule für Neurowissenschaften, Biophysik und molekulare Biowissenschaften (GGNB)de
dc.subject.gokfullBiologie (PPN619462639)de
dc.identifier.ppn869469703


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