The mitosome, a novel organelle related to mitochondria in the amitochondrial parasite Entamoeba histolytica

@article{Tovar1999TheMA,
  title={The mitosome, a novel organelle related to mitochondria in the amitochondrial parasite Entamoeba histolytica},
  author={Jorge Tovar and Anke Fischer and C. Graham Clark},
  journal={Molecular Microbiology},
  year={1999},
  volume={32}
}
Ultrastructural analysis of Entamoeba histolytica reveals that this intestinal human pathogen lacks recognizable mitochondria, but the presence in its genome of genes encoding proteins of mitochondrial origin suggests the existence of a mitochondrially derived compartment. We have cloned the full‐length E. histolytica gene encoding one such protein, chaperonin CPN60, and have characterized its structure and expression. Using an affinity‐purified antibody raised against recombinant protein, we… 
Characterization of chaperonin 10 (Cpn10) from the intestinal human pathogen Entamoeba histolytica.
TLDR
Computer-assisted protein modelling, and specific antibodies against Cpn10 and Cpn60, suggest that both proteins interact with each other, and that they function in the same intracellular compartment.
Localization and Targeting of an Unusual Pyridine Nucleotide Transhydrogenase in Entamoeba histolytica
TLDR
The data indicate that the putative targeting signal is not sufficient for the trafficking of PNT to the vesicular/vacuolar compartments and that full-length PNT is necessary for correct transport.
The Vacuolar ATPase from Entamoeba histolytica: Molecular cloning of the gene encoding for the B subunit and subcellular localization of the protein
TLDR
The isolation and characterization of the Ehvma2 gene, which encodes for the subunit B of the vacuolar ATPase of Entamoeba histolytica, and the genes encoding for the majority of the V-ATPase subunits in the E. histolyTica genome are identified, indicating the conserved nature of V- ATPase in this parasite.
Mitosomes of Entamoeba histolytica are abundant mitochondrion-related remnant organelles that lack a detectable organellar genome.
TLDR
Results indicate that a remnant organellar genome has not been retained in E. histolytica and demonstrate unequivocally that EhKOs and mitosomes are distinct and unrelated cellular structures.
The Essentials of Protein Import in the Degenerate Mitochondrion of Entamoeba histolytica
TLDR
In vitro and in vivo systems are shown that E. histolytica contains a minimalist set up of the core import components in order to accommodate a handful of mitosomal proteins, which is one of the simplest known mitochondrial compartments of all eukaryotes.
Novel mitochondrion‐related organelles in the anaerobic amoeba Mastigamoeba balamuthi
TLDR
The data indicate that the loss of classical aerobic mitochondrial functions and acquisition of anaerobic enzymes and Fe‐S cluster assembly proteins occurred in a free‐living member of the eukaryote super‐kingdom Amoebozoa.
Mitosomes in Entamoeba histolytica contain a sulfate activation pathway
TLDR
The results suggest that sulfate activation is the major function of mitosomes in E. histolytica and that E. HistolytICA mitosome represent a unique mitochondrion-related organelle with remarkable diversity.
The Minimal Proteome in the Reduced Mitochondrion of the Parasitic Protist Giardia intestinalis
TLDR
The small proteome of the Giardia mitosome reflects the reduction in mitochondrial metabolism, which is limited to the FeS cluster assembly pathway, and a simplicity in the protein import pathway required for organelle biogenesis.
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