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Orientation of FtsH protease homologs in Trypanosoma brucei inner mitochondrial membrane and its evolutionary implications
T. Kovalinka, T. Pánek, B. Kováčová, A. Horváth
Language English Country Netherlands
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Arabidopsis classification enzymology genetics MeSH
- Euglena gracilis classification enzymology genetics MeSH
- Euglena longa classification enzymology genetics MeSH
- Gene Expression MeSH
- Phylogeny MeSH
- Isoenzymes chemistry genetics metabolism MeSH
- Conserved Sequence MeSH
- Leishmania major classification enzymology genetics MeSH
- Humans MeSH
- Mitochondrial Membranes chemistry enzymology MeSH
- Mitochondrial Proteins chemistry genetics metabolism MeSH
- Mitochondria enzymology genetics MeSH
- Evolution, Molecular * MeSH
- Mice MeSH
- Peptide Hydrolases chemistry genetics metabolism MeSH
- Protein Domains MeSH
- Protozoan Proteins chemistry genetics metabolism MeSH
- Saccharomyces cerevisiae classification enzymology genetics MeSH
- Trypanosoma brucei brucei classification enzymology genetics MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
Trypanosoma brucei is an important human pathogen. In this study, we have focused on the characterization of FtsH protease, ATP-dependent membrane-bound mitochondrial enzyme important for regulation of protein abundance. We have determined localization and orientation of all six putative T.brucei FtsH homologs in the inner mitochondrial membrane by in silico analyses, by immunofluorescence, and with protease assay. The evolutionary origin of these homologs has been tested by comparative phylogenetic analysis. Surprisingly, some kinetoplastid FtsH proteins display inverted orientation in the mitochondrial membrane compared to related proteins of other examined eukaryotes. Moreover, our data strongly suggest that during evolution the orientation of FtsH protease in T. brucei varied due to both loss and acquisition of the transmembrane domain.
Faculty of Natural Sciences Comenius University Bratislava Slovakia
Faculty of Science University of Ostrava Ostrava Czech Republic
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