Bacterial-type oxygen detoxification and iron-sulfur cluster assembly in amoebal relict mitochondria

Maralikova, Barbora; Ali, Vahab; Nakada‐Tsukui, Kumiko; Nozaki, Tomoyoshi; Giezen, Mark van der; Henze, Katrin; Tovar, Jorge

doi:10.1111/j.1462-5822.2009.01397.x

Cited by 83 publications

(65 citation statements)

References 57 publications

(63 reference statements)

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“…support previous report suggesting that NIF components function in the mitosomes in addition to the cytosol of E. histolytica (18).…”

Section: Components Of E Histolytica Nif Machinery Do Not Possess Mtsupporting

confidence: 80%

“…Therefore, the predominant cytosolic distribution of the NIF machinery should be sufficient to accommodate the cellular requirements for FeS cluster biogenesis in this organism. Surprisingly, dual localization of the NIF machinery in the cytosol and the mitosomes of E. histolytica has also been suggested, and FeS cluster biogenesis has been proposed as one of the fundamental functions of entamoebal mitosomes (18). However, following proteomic analysis of E. histolytica mitosomes has not confirmed the presence of NIF machinery (20).…”

Section: Discussionmentioning

confidence: 99%

“…However, these organelles do not possess the ISC machinery, and no component of either the ISC or SUF machinery has been identified in the Entamoeba genome. NIF components have been predominantly identified in the cytosol of Entamoeba (18,19). However, it remains controversial whether these components are present exclusively in the cytosol or also operate in the mitosomes (18)(19)(20).…”

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confidence: 99%

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NIF-type iron-sulfur cluster assembly system is duplicated and distributed in the mitochondria and cytosol of Mastigamoeba balamuthi

Nývltová¹,

Šuták²,

Harant

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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In most eukaryotes, the mitochondrion is the main organelle for the formation of iron-sulfur (FeS) clusters. This function is mediated through the iron-sulfur cluster assembly machinery, which was inherited from the α-proteobacterial ancestor of mitochondria. In Archamoebae, including pathogenic Entamoeba histolytica and free-living Mastigamoeba balamuthi, the complex iron-sulfur cluster machinery has been replaced by an e-proteobacterial nitrogen fixation (NIF) system consisting of two components: NifS (cysteine desulfurase) and NifU (scaffold protein). However, the cellular localization of the NIF system and the involvement of mitochondria in archamoebal FeS assembly are controversial. Here, we show that the genes for both NIF components are duplicated within the M. balamuthi genome. One paralog of each protein contains an amino-terminal extension that targets proteins to mitochondria (NifS-M and NifU-M), and the second paralog lacks a targeting signal, thereby reflecting the cytosolic form of the NIF machinery (NifS-C and NifU-C). The dual localization of the NIF system corresponds to the presence of FeS proteins in both cellular compartments, including detectable hydrogenase activity in Mastigamoeba cytosol and mitochondria. In contrast, E. histolytica possesses only single genes encoding NifS and NifU, respectively, and there is no evidence for the presence of the NIF machinery in its reduced mitochondria. Thus, M. balamuthi is unique among eukaryotes in that its FeS cluster formation is mediated through two most likely independent NIF machineries present in two cellular compartments.hydrogenosome | mitosome | free-living protist

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“…support previous report suggesting that NIF components function in the mitosomes in addition to the cytosol of E. histolytica (18).…”

Section: Components Of E Histolytica Nif Machinery Do Not Possess Mtsupporting

confidence: 80%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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NIF-type iron-sulfur cluster assembly system is duplicated and distributed in the mitochondria and cytosol of Mastigamoeba balamuthi

Nývltová¹,

Šuták²,

Harant

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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“…In addition to the Blastocystis SUF machinery, we sought to investigate the localization and function of its putative mitochondrial ISC system previously suggested to function within its biochemically unique anaerobic MRO (12,13). The unusual properties of the Blastocystis MRO raises questions about the localization and functionality of its ISC machinery, especially because recent studies have shown that other parasitic anaerobic protists with MROs, including the microsporidian Trachipleistophora hominis and the amoebozoan Entamoeba histolytica, may have relocated some components of their Fe/S cluster biosynthetic machinery into the cytosol (7,27). Our investigations reveal that Blastocystis possesses homologues of nearly all components of the mitochondrial ISC machinery in yeast (SI Appendix, Table S1).…”

Section: Resultsmentioning

confidence: 99%

“…In eukaryotes, Fe/S proteins are assembled by several different systems, including the ISC assembly and the sulfur-mobilization (SUF) machineries, which are found only in mitochondria and plastids, respectively. Two exceptions to this rule are found in Entamoeba histolytica and Mastigamoeba balamuthi, which possess nitrogen fixation-type Fe/S systems, although the subcellular localizations of these systems remain controversial (7,8). The maturation of cytosolic and nuclear Fe/S proteins in eukaryotes is typically dependent on the cytosolic iron/sulfur assembly (CIA) machinery, which is essential in yeast and is found in all eukaryotes investigated so far (9).…”

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confidence: 99%

Evolution of Fe/S cluster biogenesis in the anaerobic parasite Blastocystis

Tsaousis

Choudens

Gentekaki

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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Iron/sulfur cluster (ISC)-containing proteins are essential components of cells. In most eukaryotes, Fe/S clusters are synthesized by the mitochondrial ISC machinery, the cytosolic iron/sulfur assembly system, and, in photosynthetic species, a plastid sulfurmobilization (SUF) system. Here we show that the anaerobic human protozoan parasite Blastocystis, in addition to possessing ISC and iron/sulfur assembly systems, expresses a fused version of the SufC and SufB proteins of prokaryotes that it has acquired by lateral transfer from an archaeon related to the Methanomicrobiales, an important lineage represented in the human gastrointestinal tract microbiome. Although components of the Blastocystis ISC system function within its anaerobic mitochondrion-related organelles and can functionally replace homologues in Trypanosoma brucei, its SufCB protein has similar biochemical properties to its prokaryotic homologues, functions within the parasite's cytosol, and is up-regulated under oxygen stress. Blastocystis is unique among eukaryotic pathogens in having adapted to its parasitic lifestyle by acquiring a SUF system from nonpathogenic Archaea to synthesize Fe/S clusters under oxygen stress.iron/sulfur cluster biosynthesis | lateral gene transfer | parasite evolution | sulfur-mobilization machinery | oxygen stress adaptation

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Entamoeba and Entamoeba histolytica

Pritt

Clark

2011

Encyclopedia of Life Sciences

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Entamoeba species are unicellular eukaryotes that parasitise all classes of vertebrates and some invertebrates. Only three species of Entamoeba have been proven to cause disease and sometimes death in their hosts: Entamoeba histolytica , a parasite of humans, Entamoeba nuttalli , a parasite of nonhuman primates and Entamoeba invadens , a parasite of reptiles. Other species appear to live as commensals in their hosts and do not cause evident disease. Amoebiasis is defined as infection with E. histolytica regardless of symptoms. Most cases of amoebiasis are asymptomatic, but E. histolytica can rarely cause intestinal or disseminated disease. Identification of E. histolytica is complicated by the existence of two morphologically identical amoebae that may also colonise the human intestinal tract, Entamoeba dispar and Entamoeba moshkovskii , neither of which are thought to cause disease. Entamoeba spp. are commonly studied to gain further insight into protozoal evolution, amoeboid locomotion and cell‐killing ability, among other topics. Key Concepts: Entamoeba species are unicellular eukaryotes in the supergroup Amoebozoa. Entamoeba species parasitise all classes of vertebrates and some invertebrates. The life cycle of most Entamoeba species consists of a motile, feeding and reproductive trophozoite stage and an environmentally resistant cyst stage responsible for transmitting the infection. Most Entamoeba species do not cause disease in their host and are considered commensal organisms. Entamoeba histolytica infection is referred to as amoebiasis regardless of whether or not symptoms are present. Most infections with E. histolytica in humans are asymptomatic, but E. histolytica can rarely cause dysentery or disseminated disease and is associated with significant human morbidity and mortality worldwide. Diagnosis and epidemiologic studies of E. histolytica are complicated by the presence of morphologically identical amoebae in human faeces. Entamoeba species are studied to gain insights into aspects of biology, including human disease, parasitism, evolution, cell locomotion and cell‐killing mechanisms.

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Bacterial-type oxygen detoxification and iron-sulfur cluster assembly in amoebal relict mitochondria

Cited by 83 publications

References 57 publications

NIF-type iron-sulfur cluster assembly system is duplicated and distributed in the mitochondria and cytosol of Mastigamoeba balamuthi

NIF-type iron-sulfur cluster assembly system is duplicated and distributed in the mitochondria and cytosol of Mastigamoeba balamuthi

Evolution of Fe/S cluster biogenesis in the anaerobic parasite Blastocystis

Entamoeba and Entamoeba histolytica

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