Analysis of Atp Synthase Super-Complex Assembly and Mitochondrial Morphology in Pcp1 Mutants
Huddleston, Mary Elizabeth
AdvisorGordon, Donna M.
CommitteeStewart Jr., James A.
Thornton, Justin A.
Mitochondria are double membraned organelles responsible for the majority of ATP production in eukaryotic cells. The mitochondrial inner membrane is folded into cristae structures and is the site of the electron transport chain which terminates in ATP generation. ATP is produced by ATP synthase, a protein complex that has also been shown to have a role in the maintenance of cristae folding. This activity is dependent on Tim11p, a subunit required for the dimerization of ATP synthase super-complexes. Additional proteins located within the inner membrane that are important to mitochondrial morphology include Pcp1p, a serine protease, and its substrate, Mgm1p. Mgm1p is required for mitochondrial fusion and cells deleted for MGM1 do not contain detectable Tim11p. Using biochemical assays and transmission electron microscopy, this study characterized pcp1 mutants in order to analyze the link between Pcp1p functionality, ATP synthase super-complex assembly, and mitochondrial morphology.