Abstract
Mitochondria are essential in eukaryotes. Besides producing 80% of total cellular ATP, mitochondria are involved in various cellular functions such as apoptosis, inflammation, innate immunity, stress tolerance, and Ca2+ homeostasis. Mitochondria are also the site for many critical metabolic pathways and are integrated into the signaling network to maintain cellular homeostasis under stress. Mitochondria require hundreds of proteins to perform all these functions. Since the mitochondrial genome only encodes a handful of proteins, most mitochondrial proteins are imported from the cytosol via receptor/translocase complexes on the mitochondrial outer and inner membranes known as TOMs and TIMs. Many of the subunits of these protein complexes are essential for cell survival in model yeast and other unicellular eukaryotes. Defects in the mitochondrial import machineries are also associated with various metabolic, developmental, and neurodegenerative disorders in multicellular organisms. In addition to their canonical functions, these protein translocases also help maintain mitochondrial structure and dynamics, lipid metabolism, and stress response. This review focuses on the role of Tim50, the receptor component of one of the TIM complexes, in different cellular functions, with an emphasis on the Tim50 homologue in parasitic protozoan Trypanosoma brucei.
Highlights
Mitochondria are evolved from the endosymbiont proteobacteria [1]
This review focuses on the structure and function of Tim50 in different eukaryotes, with an emphasis on TbTim50
Tim50 is a conserved component of the preprotein trannslocase in mitochondria
Summary
Mitochondria are evolved from the endosymbiont proteobacteria [1]. like its ancestor, mitochondria are surrounded by double membranes. Most of the mitochondrial proteins are in the MIM and the matrix require crossing both membranes [8]. Proteins are translocated through TOM and TIMs either as fully or partially unfolded conditions [8,9,10] Once reached their destination, newly translocated proteins are folded properly by for being functional. Schematics of protein complexes of the mitochondrial outer and inner membranes as identified in yeast. Mitochondrial cristae junction and the contact site for the outer and inner membranes are enlarged. Small Tim plexes acts as chaperones for hydrophobic inner membrane proteins to cross the intermembrane space. MIA40 and OXA1 complexes acts astochaperones for hydrophobic inner membrane proteins to cross the intermembrane space. OXA1 imports proteins to the intermembrane space and the inner membrane, respectively.
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