Orientation of FtsH protease homologs in Trypanosoma brucei inner mitochondrial membrane and its evolutionary implications
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
32437726
DOI
10.1016/j.molbiopara.2020.111282
PII: S0166-6851(20)30046-3
Knihovny.cz E-zdroje
- Klíčová slova
- AAA protease, Evolution, FtsH, Mitochondrion, Phylogeny, Trypanosoma,
- MeSH
- Arabidopsis klasifikace enzymologie genetika MeSH
- Euglena gracilis klasifikace enzymologie genetika MeSH
- Euglena longa klasifikace enzymologie genetika MeSH
- exprese genu MeSH
- fylogeneze MeSH
- izoenzymy chemie genetika metabolismus MeSH
- konzervovaná sekvence MeSH
- Leishmania major klasifikace enzymologie genetika MeSH
- lidé MeSH
- mitochondriální membrány chemie enzymologie MeSH
- mitochondriální proteiny chemie genetika metabolismus MeSH
- mitochondrie enzymologie genetika MeSH
- molekulární evoluce * MeSH
- myši MeSH
- proteasy chemie genetika metabolismus MeSH
- proteinové domény MeSH
- protozoální proteiny chemie genetika metabolismus MeSH
- Saccharomyces cerevisiae klasifikace enzymologie genetika MeSH
- Trypanosoma brucei brucei klasifikace enzymologie genetika MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- izoenzymy MeSH
- mitochondriální proteiny MeSH
- proteasy MeSH
- protozoální proteiny 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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