Fe–S cluster assembly in the supergroup Excavata

Peña-Diaz, Priscila; Lukeš, Julius

doi:10.1007/s00775-018-1556-6

Cited by 21 publications

(7 citation statements)

References 252 publications

(406 reference statements)

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“…Another hypothesis, which does not exclude others, suggests that the reason for the existence of mitochondria could have been the assembly of Fe/S clusters (Lill et al, 1999), the latter being the only mitochondrial biosynthetic pathway that is essential for survival of eukaryotic cells. So far, this has been shown experimentally in yeast (Braymer and Lill, 2017), mammalian cells (Rouault and Maio, 2017), and trypanosomes (Pena-Diaz and Lukes, 2018).…”

Section: Iron-sulfur Cluster Assembly In Mitochondrial Diversitymentioning

confidence: 81%

On the Origin of Iron/Sulfur Cluster Biosynthesis in Eukaryotes

Tsaousis

2019

Front. Microbiol.

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Iron and sulfur are indispensable elements of every living cell, but on their own these elements are toxic and require dedicated machineries for the formation of iron/sulfur (Fe/S) clusters. In eukaryotes, proteins requiring Fe/S clusters (Fe/S proteins) are found in or associated with various organelles including the mitochondrion, endoplasmic reticulum, cytosol, and the nucleus. These proteins are involved in several pathways indispensable for the viability of each living cell including DNA maintenance, protein translation and metabolic pathways. Thus, the formation of Fe/S clusters and their delivery to these proteins has a fundamental role in the functions and the evolution of the eukaryotic cell. Currently, most eukaryotes harbor two (located in cytosol and mitochondrion) or three (located in plastid) machineries for the assembly of Fe/S clusters, but certain anaerobic microbial eukaryotes contain sulfur mobilization (SUF) machineries that were previously thought to be present only in archaeal linages. These machineries could not only stipulate which pathway was present in the last eukaryotic common ancestor (LECA), but they could also provide clues regarding presence of an Fe/S cluster machinery in the proto-eukaryote and evolution of Fe/S cluster assembly machineries in all eukaryotes.

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Section: Iron-sulfur Cluster Assembly In Mitochondrial Diversitymentioning

confidence: 81%

On the Origin of Iron/Sulfur Cluster Biosynthesis in Eukaryotes

Tsaousis

2019

Front. Microbiol.

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“…In most eukaryotes, the first step, referred to as ISC biosynthesis, is located in the mitochondrion ( Braymer and Lill 2017 ). Among euglenozoans, Fe-S cluster assembly is best studied in T. brucei , whereas in the euglenids and diplonemids, the pathway remains unexplored ( Ali and Nozaki 2013 ; Peña-Diaz and Lukeš 2018 ). We find conservation of all predicted central components of this pathway, with some notable expansions.…”

Section: Resultsmentioning

confidence: 99%

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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“…There is also evidence indicating that the benefit provided by the first mitochondrial endosymbiont was the generation of heat, enabling the host to colonize cooler environments with a higher internal temperature maintaining membrane fluidity, DNA helical tension, enzymatic reaction rates and other temperature-dependent cellular processes [ 40 ]. It has been postulated that assembly of Fe–S clusters was the essential contribution of the endosymbiont and the reason for the existence of the mitochondrion [ 44 , 45 ], as Fe–S cluster synthesis is essential for eukaryotic cell survival [ [46] , [47] , [48] ]. Others have proposed a non-mutualistic scenario, where the proto-mitochondrion was a predator invading the host [ 49 , 50 ].…”

Section: Mitochondria and Endosymbiosismentioning

confidence: 99%

Mitochondrial iron–sulfur clusters: Structure, function, and an emerging role in vascular biology

et al. 2021

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Iron-sulfur (Fe–S) clusters are essential cofactors most commonly known for their role mediating electron transfer within the mitochondrial respiratory chain. The Fe–S cluster pathways that function within the respiratory complexes are highly conserved between bacteria and the mitochondria of eukaryotic cells. Within the electron transport chain, Fe–S clusters play a critical role in transporting electrons through Complexes I, II and III to cytochrome c , before subsequent transfer to molecular oxygen. Fe–S clusters are also among the binding sites of classical mitochondrial inhibitors, such as rotenone, and play an important role in the production of mitochondrial reactive oxygen species (ROS). Mitochondrial Fe–S clusters also play a critical role in the pathogenesis of disease. High levels of ROS produced at these sites can cause cell injury or death, however, when produced at low levels can serve as signaling molecules. For example, Ndufs2, a Complex I subunit containing an Fe–S center, N2, has recently been identified as a redox-sensitive oxygen sensor, mediating homeostatic oxygen-sensing in the pulmonary vasculature and carotid body. Fe–S clusters are emerging as transcriptionally-regulated mediators in disease and play a crucial role in normal physiology, offering potential new therapeutic targets for diseases including malaria, diabetes, and cancer.

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Fe–S cluster assembly in the supergroup Excavata

Cited by 21 publications

References 252 publications

On the Origin of Iron/Sulfur Cluster Biosynthesis in Eukaryotes

On the Origin of Iron/Sulfur Cluster Biosynthesis in Eukaryotes

A Uniquely Complex Mitochondrial Proteome from Euglena gracilis

Mitochondrial iron–sulfur clusters: Structure, function, and an emerging role in vascular biology

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