title: Highly divergent mitochondrion-related organelles in anaerobic parasitic protozoa.
abstract: The mitochondria have arisen as a consequence of endosymbiosis of an ancestral α-proteobacterium with a methane-producing archae. The main function of the canonical aerobic mitochondria include ATP generation via oxidative phosphorylation, heme and phospholipid synthesis, calcium homeostasis, programmed cell death, and the formation of iron-sulfur clusters. Under oxygen-restricted conditions, the mitochondrion has often undergone remarkable reductive alterations of its content and function, leading to the generation of mitochondrion-related organelles (MROs), such as mitosomes, hydrogenosomes, and mithochondrion-like organelles, which are found in a wide range of anaerobic/microaerophilic eukaryotes that include several medically important parasitic protists such as Entamoeba histolytica, Giardia intestinalis, Trichomonas vaginalis, Cryptosporidium parvum, Blastocystis hominis, and Encephalitozoon cuniculi, as well as free-living protists such as Sawyeria marylandensis, Neocallimastix patriciarum, and Mastigamoeba balamuthi. The transformation from canonical aerobic mitochondria to MROs apparently have occurred in independent lineages, and resulted in the diversity of their components and functions. Due to medical and veterinary importance of the MRO-possessing human- and animal-pathogenic protozoa, their genomic, transcriptomic, proteomic, and biochemical evidence has been accumulated. Detailed analyses of the constituents and functions of the MROs in such anaerobic pathogenic protozoa, which reside oxygen-deprived or oxygen-poor environments such as the mammalian intestine and the genital organs, should illuminate the current evolutionary status of the MROs in these organisms, and give insight to environmental constraints that drive the evolution of eukaryotes and their organelles. In this review, we summarize and discuss the diverse metabolic functions and protein transport systems of the MROs from anaerobic parasitic protozoa.
authors: Department of Infectious Diseases, Tokai University School of Medicine, Isehara, Kanagawa 259-1193, Japan; Department of Parasitology, National Institute of Infectious Diseases, 1-23-1 Toyama, Shinjuku-ku, Tokyo 162-8640, Japan.
authors: Takashi
authors: T
authors: Makiuchi
authors: Department of Parasitology, National Institute of Infectious Diseases, 1-23-1 Toyama, Shinjuku-ku, Tokyo 162-8640, Japan; Graduate School of Life and Environmental Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8572, Japan. Electronic address: nozaki@nih.go.jp.
authors: Tomoyoshi
authors: T
authors: Nozaki
mesh_terms: D056893:Alveolata / Q000502:physiology / Q000648:ultrastructure; D056894:Amoebozoa / Q000502:physiology / Q000648:ultrastructure; D000693:Anaerobiosis; D044822:Biodiversity; D005075:Biological Evolution; D044785:Cryptophyta / Q000502:physiology / Q000648:ultrastructure; D016828:Diplomonadida / Q000502:physiology / Q000648:ultrastructure; D005786:Gene Expression Regulation; D054629:Genome, Mitochondrial; D006801:Humans; D008928:Mitochondria / Q000235:genetics* / Q000378:metabolism* / Q000648:ultrastructure; D024101:Mitochondrial Proteins / Q000235:genetics / Q000378:metabolism*; D020088:Neocallimastix / Q000502:physiology / Q000648:ultrastructure; D010802:Phylogeny; D021381:Protein Transport
chemical_list: D024101:Mitochondrial Proteins
keywords: Evolution; Hydrogenosome; Mitochondria; Mitochondrion-related organelles; Mitosome; Parasite