Tim17 Updates: A Comprehensive Review of an Ancient Mitochondrial Protein Translocator

• Published in: Biomolecules (Basel, Switzerland) Vol. 10; no. 12; p. 1643
• Main Authors: Chaudhuri, Minu, Darden, Chauncey, Gonzalez, Fidel Soto, Singha, Ujjal K, Quinones, Linda, Tripathi, Anuj
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 07.12.2020; MDPI
• Subjects: Cooperativity; Fungi; Genomes; Inner membranes; Mammals; Membranes; Mitochondria; protein import; Proteins; Protozoa; Review; Structure-function relationships; TIM; Tim17; TOM; trypanosomes; TIM; TOM; protein import; trypanosomes; mitochondria; Tim17
• ISSN: 2218-273X; 2218-273X
• DOI: 10.3390/biom10121643

The translocases of the mitochondrial outer and inner membranes, the TOM and TIMs, import hundreds of nucleus-encoded proteins into mitochondria. TOM and TIMs are multi-subunit protein complexes that work in cooperation with other complexes to import proteins in different sub-mitochondrial destinations. The overall architecture of these protein complexes is conserved among yeast/fungi, animals, and plants. Recent studies have revealed unique characteristics of this machinery, particularly in the eukaryotic supergroup Excavata. Despite multiple differences, homologues of Tim17, an essential component of one of the TIM complexes and a member of the Tim17/Tim22/Tim23 family, have been found in all eukaryotes. Here, we review the structure and function of Tim17 and Tim17-containing protein complexes in different eukaryotes, and then compare them to the single homologue of this protein found in , a unicellular parasitic protozoan.