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Lookup NU author(s): Dr Eva Heinz
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Mitochondria are present in all eukaryotes, but remodeling of their metabolic contribution has in some cases left them almost unrecognizable and they are referred to as mitochondria-like organelles, hydrogenosomes or, in the case where evolution has led to a great deal of simplification, as mitosomes. Mitochondria rely on the import of proteins encoded in the nucleus and the protein import machinery has been investigated in detail in yeast: several sophisticated molecular machines act in concert to import substrate proteins across the outer mitochondrial membrane and deliver them to a precise sub-mitochondrial compartment. Because these machines are so sophisticated, it has been a major challenge to conceptualize the first phase of their evolution. Here we review recent studies on the protein import pathway in parasitic species that have mitosomes: in the course of their evolution for highly specialized niches these parasites, particularly Cryptosporidia and Microsporidia, have secondarily lost numerous protein functions, in accordance with the evolution of their genomes towards a minimal size. Microsporidia are related to fungi, Cryptosporidia are apicomplexans and kin to the malaria parasite Plasmodium; and this great phylogenetic distance makes it remarkable that Microsporidia and Cryptosporidia have independently evolved skeletal protein import pathways that are almost identical. We suggest that the skeletal pathway reflects the protein import machinery of the first eulcaryotes, and defines the essential roles of the core elements of the mitochondrial protein import machinery. This article is part of a Special Issue entitled: Protein Import and Quality Control in Mitochondria and Plastids. (C) 2012 Elsevier B.V. All rights reserved.
Author(s): Heinz E, Lithgow T
Publication type: Review
Publication status: Published
Journal: Biochimica et Biophysica Acta - Molecular Cell Research
Year: 2013
Volume: 1833
Issue: 2
Pages: 295-303
Print publication date: 16/02/2013
ISSN (print): 0167-4889
ISSN (electronic):
Publisher: ELSEVIER SCIENCE BV
URL: http://dx.doi.org/10.1016/j.bbamcr.2012.02.006
DOI: 10.1016/j.bbamcr.2012.02.006
