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

Levchenko, Mariia

dc.contributor.advisor	Rehling, Peter Prof. Dr.
dc.contributor.author	Levchenko, Mariia
dc.date.accessioned	2016-09-05T09:09:00Z
dc.date.available	2016-09-05T09:09:00Z
dc.date.issued	2016-09-05
dc.identifier.uri	http://hdl.handle.net/11858/00-1735-0000-0028-8824-B
dc.identifier.uri	http://dx.doi.org/10.53846/goediss-5841
dc.language.iso	eng	de
dc.rights.uri	http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subject.ddc	572	de
dc.title	Mitochondrial protein assemblies: Biogenesis of the cytochrome c oxidase and mitophagic signaling complexes	de
dc.type	doctoralThesis	de
dc.contributor.referee	Rehling, Peter Prof. Dr.
dc.date.examination	2015-12-02
dc.description.abstracteng	Mitochondrial 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.coReferee	Schwappach, Blanche Prof. Dr.
dc.subject.eng	mitochondria	de
dc.subject.eng	mitophagy	de
dc.subject.eng	Atg32	de
dc.subject.eng	Cox26	de
dc.subject.eng	mitochondrial degradation	de
dc.subject.eng	mitochondrial quality control	de
dc.subject.eng	cytochrome c oxidase	de
dc.subject.eng	supercomplexes	de
dc.subject.eng	respiration	de
dc.subject.eng	COX assembly	de
dc.identifier.urn	urn:nbn:de:gbv:7-11858/00-1735-0000-0028-8824-B-6
dc.affiliation.institute	Göttinger Graduiertenschule für Neurowissenschaften, Biophysik und molekulare Biowissenschaften (GGNB)	de
dc.subject.gokfull	Biologie (PPN619462639)	de
dc.identifier.ppn	869469703

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GGNB - Göttinger Graduiertenzentrum für Neurowissenschaften, Biophysik und molekulare Biowissenschaften [1112]
GGNB - Göttingen Graduate Center for Neurosciences, Biophysics and Molecular Biosciences

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