Faculty of Natural Sciences, Comenius University, Bratislava, Slovakia.
Faculty of Science, University of Ostrava, Ostrava, Czech Republic.
Mol Biochem Parasitol. 2020 Jul;238:111282. doi: 10.1016/j.molbiopara.2020.111282. Epub 2020 May 11.
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.
布氏锥虫是一种重要的人类病原体。在这项研究中，我们专注于 FtsH 蛋白酶的特性研究，这是一种重要的依赖于 ATP 的膜结合线粒体酶，对于调节蛋白质丰度具有重要作用。我们通过计算机分析、免疫荧光和蛋白酶检测，确定了内线粒体膜中所有六个推定的 T. brucei FtsH 同源物的定位和方向。通过比较系统发育分析测试了这些同源物的进化起源。令人惊讶的是，与其他被检查的真核生物的相关蛋白相比，一些动基体锥虫 FtsH 蛋白在线粒体膜中显示出倒置的方向。此外，我们的数据强烈表明，在进化过程中，由于跨膜结构域的丢失和获得，FtsH 蛋白酶在 T. brucei 中的方向发生了变化。
