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- W3166382246 abstract "Alternative editing of the cytochrome c oxidase III pre-mRNA in Trypanosoma brucei (T. brucei) produces a novel mitochondrial membrane protein, alternatively edited protein-1 (AEP-1). Immunofluorescence microscopy reveals that this unique protein associates with two distinct regions intracellularly. AEP-1 is distributed throughout the mitochondria and is also observable as a discrete condensed structure associated with the detergent resistant tripartite attachment complex adjacent to the mitochondrial DNA. Biochemical fractionation and Blue Native PAGE (BNPAGE) analysis has also shown that AEP-1 associates with the detergent soluble mitochondrial membranes. To further investigate the role of AEP-1 localized to the mitochondrial membrane, intact mitochondria were isolated using a hypotonic lysis method and the organelles were treated with a tandem nonionic detergent treatment to separate the mitochondrial matrix from the membrane fraction. Separation of this membrane fraction by BNPAGE and Western Blot analysis revealed the association of AEP-1 with a high molecular weight membrane complex. The AEP-1 complex was purified further using anion exchange chromatography and the resulting BNPAGE band was subjected to ESI-ion trap-tandem mass spectrometry. Sequencing revealed several proteins including the oxoglutarate dehydrogenase (E1) and the dihydrolipoyl succinyltransferase (E2) subunits of the 2-oxoglutarate dehydrogenase complex (2ODC). The AEP-1 complex did not retain the same NAD+reductive capacity as the bonafide 2ODC. These data suggest that AEP-1 associates with proteins that may have bifunctional roles in T. brucei mitochondria." @default.
- W3166382246 created "2021-06-22" @default.
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- W3166382246 date "2010-04-01" @default.
- W3166382246 modified "2023-09-26" @default.
- W3166382246 title "Alternative Editing of Cytochrome C Oxidase III mRNA in Trypanosome Mitochondria Generates Protein Diversity" @default.
- W3166382246 doi "https://doi.org/10.1096/fasebj.24.1_supplement.497.1" @default.
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