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dc.contributor.authorGulde, Paul Elliot
dc.date.accessioned2016-03-29T17:18:46Z
dc.date.available2016-03-29T17:18:46Z
dc.date.issued2010
dc.identifier.isbn9781109625417
dc.identifier.other305238303
dc.identifier.urihttp://hdl.handle.net/10477/45932
dc.description.abstractThe Trypanosoma brucei ATP synthase functions as a hydrolase in bloodstream form parasites and as a synthase in the procyclic form parasites. The dual functionality of the complex enables the parasite to maintain the membrane potential in both environments. This study focuses on the role of the F 0 component subunit 9 in the structure, function and regulation of the ATP synthase. We have shown that the T. brucei produces two isoforms of S9 (S9-1 and S9-2). Each isoform is differentially regulated. Both isoforms are incorporated into the ATP synthase, within the same F 0 component. Expression of each isoform was decreased by RNA interference, however, S9-2 increased initially in response to RNAi before ultimately decreasing. Loss of S9 results in a loss in the ATP synthase complex and, interestingly, a loss in the complexes of the electron transport chain. This results in an unexpected loss of membrane potential in the procyclic cells. Loss of S9 also results in a decrease in the α and β subunits expression at the transcript and protein levels. This suggests that S9 plays a major role in the regulation of the ATP synthase and other mitochondrial complexes.
dc.languageEnglish
dc.sourceDissertations & Theses @ SUNY Buffalo,ProQuest Dissertations & Theses Global
dc.subjectBiological sciences
dc.subjectATP synthase
dc.subjectSubunit 9
dc.subjectTrypanosoma brucei
dc.titleThe role of subunit 9 in the structure, function and regulation of the Trypanosoma brucei ATP synthase
dc.typeDissertation/Thesis


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