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A novel ADP/ATP transporter in the mitosome of the microaerophilic human parasite Entamoeba histolytica

Lookup NU author(s): Emeritus Professor T. Martin Embley FMedSci FRSORCiD

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Abstract

Recent data suggest that microaerophilic and parasitic protozoa, which lack oxidative phosphorylation, nevertheless contain mitochondrial homologs [1-6], organelles that share common ancestry with mitochondria. Such widespread retention suggests there may be a common function for mitochondrial homologs that makes them essential for eukaryotic cells. We determined the mitochondrial carrier family (MCF) complement of the Entamoeba histolytica mitochondrial homolog, also known as a crypton [5] or more commonly as a mitosome [3]. MCF proteins support mitochondrial metabolic energy generation, DNA replication, and amino-acid metabolism by linking biochemical pathways in the mitochondrial matrix with those in the cytosol [7]. MCF diversity thus closely mirrors important facets of mitochondrial metabolic diversity. The Entamoeba histolytica mitosome has lost all but a single type of MCF protein, which transports ATP and ADP via a novel mechanism that is not reliant on a membrane potential. Phylogenetic analyses confirm that the Entamoeba ADP/ATP carrier is distinct from archetypal mitochondrial ADP/ATP carriers, an observation that is supported by its different substrate and inhibitor specificity. Because many functions of yeast and human mitochondria rely on solutes transported by specialized members of this family, the Entamoeba mitosome must contain only a small subset of these processes requiring adenine nucleotide exchange. ©2005 Elsevier Ltd. All rights reserved.

Publication metadata

Author(s): Chan KW, Slotboom D-J, Cox S, Embley TM, Fabre O, Van Der Giezen M, Harding M, Horner DS, Kunji ERS, Leon-Avila G, Tovar J

Publication type: Article

Publication status: Published

Journal: Current Biology

Year: 2005

Volume: 15

Issue: 8

Pages: 737-742

Print publication date: 26/04/2005

ISSN (print): 0960-9822

ISSN (electronic): 1879-0445

Publisher: Cell Press

URL: http://dx.doi.org/10.1016/j.cub.2005.02.068

DOI: 10.1016/j.cub.2005.02.068

PubMed id: 15854906

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