Identification of the mitochondrially encoded subunit 6 of F1FO ATPase in Trypanosoma brucei

Škodová-Sveráková, Ingrid; Horváth, Anton; Maslov, Dmitri

doi:10.1016/j.molbiopara.2015.08.002

Cited by 16 publications

(17 citation statements)

References 23 publications

(30 reference statements)

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“…In trypanosomes, recovery of these complexes has required specific extraction procedures ( Horváth et al. 2000 ; Škodová-Sveráková et al. 2015 ), and hence detection of five mitochondrially encoded proteins is notable and further demonstrates the quality of our data set.…”

Section: Resultsmentioning

confidence: 81%

A Uniquely Complex Mitochondrial Proteome from Euglena gracilis

Hammond

Nenarokova

Butenko

et al. 2020

Molecular Biology and Evolution

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Euglena gracilis is a metabolically flexible, photosynthetic, and adaptable free-living protist of considerable environmental importance and biotechnological value. By label-free liquid chromatography tandem mass spectrometry, a total of 1,786 proteins were identified from the E. gracilis purified mitochondria, representing one of the largest mitochondrial proteomes so far described. Despite this apparent complexity, protein machinery responsible for the extensive RNA editing, splicing, and processing in the sister clades diplonemids and kinetoplastids is absent. This strongly suggests that the complex mechanisms of mitochondrial gene expression in diplonemids and kinetoplastids occurred late in euglenozoan evolution, arising independently. By contrast, the alternative oxidase pathway and numerous ribosomal subunits presumed to be specific for parasitic trypanosomes are present in E. gracilis. We investigated the evolution of unexplored protein families, including import complexes, cristae formation proteins, and translation termination factors, as well as canonical and unique metabolic pathways. We additionally compare this mitoproteome with the transcriptome of Eutreptiella gymnastica, illuminating conserved features of Euglenida mitochondria as well as those exclusive to E. gracilis. This is the first mitochondrial proteome of a free-living protist from the Excavata and one of few available for protists as a whole. This study alters our views of the evolution of the mitochondrion and indicates early emergence of complexity within euglenozoan mitochondria, independent of parasitism.

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Section: Resultsmentioning

confidence: 81%

A Uniquely Complex Mitochondrial Proteome from Euglena gracilis

Hammond

Nenarokova

Butenko

et al. 2020

Molecular Biology and Evolution

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“…While de novo mt synthesis of cytochrome b, cytochrome oxidase subunit 1 and F o F 1 -ATP synthase subunit A6 can be observed in PF parasites, none of the highly hydrophobic mt encoded proteins have ever been detected in the BF mitochondrion 20 . Therefore, to circumvent the dearth of direct assays to measure mt translation in the dKO TbMrf1 cell line, we opted to investigate the structural integrity of the mitoribosomes and F o F 1 -ATPase.…”

Section: Resultsmentioning

confidence: 93%

“…A similar indispensable role is assumed for the T. brucei RPS12 because the inactivation of RNA editing leads to the reduction of the 45S SSU-related complex and the 80S mRNA-bound monosome 7 . Furthermore, while only a few (cytochrome b, cytochrome oxidase subunit 1, F o F 1 -ATP synthase subunit A6) of the highly hydrophobic proteins translated from the maxicircle transcripts can be reliably detected in just procyclic form parasites 19 , 20 , the disruption of RNA editing severely impairs mitochondrial translation. Therefore, it is proposed that RPS12 acts as a functional link between RNA editing and translation in T. brucei 7 .…”

Section: Introductionmentioning

confidence: 99%

Cultured bloodstream Trypanosoma brucei adapt to life without mitochondrial translation release factor 1

Procházková

Panicucci

Zı́ková

2018

Sci Rep

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Trypanosoma brucei is an extracellular parasite that alternates between an insect vector (procyclic form) and the bloodstream of a mammalian host (bloodstream form). While it was previously reported that mitochondrial release factor 1 (TbMrf1) is essential in cultured procyclic form cells, we demonstrate here that in vitro bloodstream form cells can tolerate the elimination of TbMrf1. Therefore, we explored if this discrepancy is due to the unique bioenergetics of the parasite since procyclic form cells rely on oxidative phosphorylation; whereas bloodstream form cells utilize glycolysis for ATP production and FoF1-ATPase to maintain the essential mitochondrial membrane potential. The observed disruption of intact bloodstream form FoF1-ATPases serves as a proxy to indicate that the translation of its mitochondrially encoded subunit A6 is impaired without TbMrf1. While these null mutants have a decreased mitochondrial membrane potential, they have adapted by increasing their dependence on the electrogenic contributions of the ADP/ATP carrier to maintain the mitochondrial membrane potential above the minimum threshold required for T. brucei viability in vitro. However, this inefficient compensatory mechanism results in avirulent mutants in mice. Finally, the depletion of the codon-independent release factor TbPth4 in the TbMrf1 knockouts further exacerbates the characterized mitchondrial phenotypes.

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“…Upon the addition of complex poly-U/A tails 27, 28 ( Figure 4), the fully edited transcripts are translated on protein-rich and rRNA-poor ribosomes 39 , but the role of the additional 45S ribosomal subunit of unique protein composition is still unclear 40 . Likely owing to their extreme hydrophobicity, only a few of the de novo synthesized mt proteins have been observed 41, 42 .…”

Section: Mechanisms Of Mitochondrial Gene Expressionmentioning

confidence: 99%

From simple to supercomplex: mitochondrial genomes of euglenozoan protists

et al. 2016

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Mitochondria are double membrane organelles of endosymbiotic origin, best known for constituting the centre of energetics of a eukaryotic cell. They contain their own mitochondrial genome, which as a consequence of gradual reduction during evolution typically contains less than two dozens of genes. In this review, we highlight the extremely diverse architecture of mitochondrial genomes and mechanisms of gene expression between the three sister groups constituting the phylum Euglenozoa - Euglenida, Diplonemea and Kinetoplastea. The earliest diverging euglenids possess a simplified mitochondrial genome and a conventional gene expression, whereas both are highly complex in the two other groups. The expression of their mitochondrial-encoded proteins requires extensive post-transcriptional modifications guided by complex protein machineries and multiple small RNA molecules. Moreover, the least studied diplonemids, which have been recently discovered as a highly abundant component of the world ocean plankton, possess one of the most complicated mitochondrial genome organisations known to date.

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Identification of the mitochondrially encoded subunit 6 of F1FO ATPase in Trypanosoma brucei

Cited by 16 publications

References 23 publications

A Uniquely Complex Mitochondrial Proteome from Euglena gracilis

A Uniquely Complex Mitochondrial Proteome from Euglena gracilis

Cultured bloodstream Trypanosoma brucei adapt to life without mitochondrial translation release factor 1

From simple to supercomplex: mitochondrial genomes of euglenozoan protists

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