FMT, a protein that affects mitochondrial distribution, interacts with translation-related proteins in Arabidopsis thaliana

• Published in: Plant cell reports 2021-02, Vol.40 (2), p.327-337
• Main Authors: Ayabe, Hiroki, Kawai, Narumi, Shibamura, Mitsuhiro, Fukao, Yoichiro, Fujimoto, Masaru, Tsutsumi, Nobuhiro, Arimura, Shin-ichi
• Format: Article
• Language: English
• Subjects: Actin; Actin Cytoskeleton - metabolism; Alleles; Arabidopsis - genetics; Arabidopsis - physiology; Arabidopsis - ultrastructure; Arabidopsis Proteins - genetics; Arabidopsis Proteins - metabolism; Arabidopsis thaliana; Biomedical and Life Sciences; Biotechnology; Cell Biology; Cytosol; Cytosol - metabolism; Divergence; Environmental factors; Eukaryotic Initiation Factor-4G - genetics; Eukaryotic Initiation Factor-4G - metabolism; Filaments; Genes; Genes, Reporter; Glutamate-tRNA ligase; Life Sciences; Microtubules; Microtubules - metabolism; Microtubules - ultrastructure; Mitochondria; Mitochondria - metabolism; Mitochondria - ultrastructure; Mitochondrial Proteins - genetics; Mitochondrial Proteins - metabolism; Mutants; Mutation; Original Article; Plant Biochemistry; Plant Sciences; Proteins; RNA-Binding Proteins - genetics; RNA-Binding Proteins - metabolism; Translation; tRNA; Two-Hybrid System Techniques; Yeasts
• ISSN: 0721-7714; 1432-203X
• DOI: 10.1007/s00299-020-02634-9

Key message Two translation-related proteins are identified as FMT-interacting proteins. However, FMT, unlike mutants of other CLU genes in fly and human, has no clear impact on the accumulation of mitochondrial proteins. Organelle distribution is critical for effective metabolism and stress response and is controlled by various environmental factors. Clustered mitochondria ( CLU ) superfamily genes affect mitochondrial distribution and their disruptions cause mitochondria to cluster within a cell in various species including yeast, fly, mammals and Arabidopsis . In Arabidopsis thaliana , Friendly mitochondria ( FMT ) is a CLU gene that is required for normal mitochondrial distribution, but its molecular function is unclear. Here, we demonstrate that FMT interacts with some translation-related proteins (translation initiation factor eIFiso4G1 and glutamyl-tRNA synthetase OVA9), as well as itself. We also show FMT forms dynamic particles in the cytosol that sometimes move with mitochondria, and their movements are mainly controlled by actin filaments but also by microtubules. Similar results have been reported for animal CLU orthologs. However, an fmt mutant, unlike animal clu mutants, did not show any clear decrease of nuclear-encoded mitochondrial protein levels. This difference may reflect a functional divergence of FMT from other CLU superfamily genes.