NDLI: Divergent molecular evolution of the mitochondrial sulfhydryl:cytochrome C oxidoreductase Erv in opisthokonts and parasitic protists.

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Divergent molecular evolution of the mitochondrial sulfhydryl:cytochrome C oxidoreductase Erv in opisthokonts and parasitic protists.

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Divergent molecular evolution of the mitochondrial sulfhydryl:cytochrome C oxidoreductase Erv in opisthokonts and parasitic protists.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Gross, Dominik Hell, Kai Riemer, Jan Deponte, Marcel Eckers, Elisabeth Petrungaro, Carmelina
Description	Author Affiliation: Eckers E ( Department of Parasitology, Ruprecht-Karls University, Im Neuenheimer Feld 324, D-69120 Heidelberg, Germany.)
Abstract	Mia40 and the sulfhydryl:cytochrome c oxidoreductase Erv1/ALR are essential for oxidative protein import into the mitochondrial intermembrane space in yeast and mammals. Although mitochondrial protein import is functionally conserved in the course of evolution, many organisms seem to lack Mia40. Moreover, except for in organello import studies and in silico analyses, nothing is known about the function and properties of protist Erv homologues. Here we compared Erv homologues from yeast, the kinetoplastid parasite Leishmania tarentolae, and the non-related malaria parasite Plasmodium falciparum. Both parasite proteins have altered cysteine motifs, formed intermolecular disulfide bonds in vitro and in vivo, and could not replace Erv1 from yeast despite successful mitochondrial protein import in vivo. To analyze its enzymatic activity, we established the expression and purification of recombinant full-length L. tarentolae Erv and compared the mechanism with related and non-related flavoproteins. Enzyme assays indeed confirmed an electron transferase activity with equine and yeast cytochrome c, suggesting a conservation of the enzymatic activity in different eukaryotic lineages. However, although Erv and non-related flavoproteins are intriguing examples of convergent molecular evolution resulting in similar enzyme properties, the mechanisms of Erv homologues from parasitic protists and opisthokonts differ significantly. In summary, the Erv-mediated reduction of cytochrome c might be highly conserved throughout evolution despite the apparent absence of Mia40 in many eukaryotes. Nevertheless, the knowledge on mitochondrial protein import in yeast and mammals cannot be generally transferred to all other eukaryotes, and the corresponding pathways, components, and mechanisms remain to be analyzed.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	4
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-01-25
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cytochrome Reductases Chemistry Cytochromes c Mitochondrial Proteins Physiology Oxidoreductases Acting On Sulfur Group Donors Oxidoreductases Saccharomyces Cerevisiae Proteins Amino Acid Sequence Animals Cell Lineage Computational Biology Electrons Genetic Complementation Test Kinetics Kinetoplastida Metabolism Leishmania Mitochondria Genetics Molecular Conformation Molecular Sequence Data Mutagenesis, Site-Directed Plasmodium Protein Transport Saccharomyces Cerevisiae Sequence Homology, Amino Acid Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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