Iron–Sulphur Clusters, Their Biosynthesis, and Biological Functions in Protozoan Parasites

Ali, Vahab; Nozaki, Tomoyoshi

doi:10.1016/b978-0-12-407705-8.00001-x

Cited by 34 publications

(28 citation statements)

References 344 publications

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“…With these two cytosolic Fe/S cluster biogenesis systems, the Blastocystis sp. resembles Entamoeba and Mastigamoeba, both of which possess novel cytosolic NIF systems (16,31), in addition to CIA components (presumed to be cytosolic in these organisms) ( Table 1). For these organisms, it is unclear how Fe/S cluster biogenesis is partitioned between the two cytosolic systems and whether or not they function independently or in a coordinated fashion.…”

Section: Resultsmentioning

confidence: 99%

Evolution of the Cytosolic Iron-Sulfur Cluster Assembly Machinery in Blastocystis Species and Other Microbial Eukaryotes

et al. 2014

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bThe cytosolic iron/sulfur cluster assembly (CIA) machinery is responsible for the assembly of cytosolic and nuclear iron/sulfur clusters, cofactors that are vital for all living cells. This machinery is uniquely found in eukaryotes and consists of at least eight proteins in opisthokont lineages, such as animals and fungi. We sought to identify and characterize homologues of the CIA system proteins in the anaerobic stramenopile parasite Blastocystis sp. strain NandII. We identified transcripts encoding six of the components-Cia1, Cia2, MMS19, Nbp35, Nar1, and a putative Tah18 -and showed using immunofluorescence microscopy, immunoelectron microscopy, and subcellular fractionation that the last three of them localized to the cytoplasm of the cell. We then used comparative genomic and phylogenetic approaches to investigate the evolutionary history of these proteins. While most Blastocystis homologues branch with their eukaryotic counterparts, the putative Blastocystis Tah18 seems to have a separate evolutionary origin and therefore possibly a different function. Furthermore, our phylogenomic analyses revealed that all eight CIA components described in opisthokonts originated before the diversification of extant eukaryotic lineages and were likely already present in the last eukaryotic common ancestor (LECA). The Nbp35, Nar1 Cia1, and Cia2 proteins have been conserved during the subsequent evolutionary diversification of eukaryotes and are present in virtually all extant lineages, whereas the other CIA proteins have patchy phylogenetic distributions. Cia2 appears to be homologous to SufT, a component of the prokaryotic sulfur utilization factors (SUF) system, making this the first reported evolutionary link between the CIA and any other Fe/S biogenesis pathway. All of our results suggest that the CIA machinery is an ubiquitous biosynthetic pathway in eukaryotes, but its apparent plasticity in composition raises questions regarding how it functions in nonmodel organisms and how it interfaces with various iron/sulfur cluster systems (i.e., the iron/sulfur cluster, nitrogen fixation, and/or SUF system) found in eukaryotic cells.

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Section: Resultsmentioning

confidence: 99%

Evolution of the Cytosolic Iron-Sulfur Cluster Assembly Machinery in Blastocystis Species and Other Microbial Eukaryotes

et al. 2014

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“…As an unorthodox cytoplasmic ABC/ATPase, Suf-C is required for Fe-S cluster biogenesis under oxidative stress in Escherichia coli (Loiseau et al 2003). Iron-sulfur clusters participate in the process of electron transfer, substrate binding/activation, iron-sulfur storage and regulation of gene expression (Ali and Nozaki 2013;Johnson et al 2005). In E. coli, Suf and Isc can both assemble Fe-S clusters, but the Suf pathway is the better choice under oxidative stress and iron starvation conditions (Ayala-Castro et al 2008).…”

Section: Oxidative Responsementioning

confidence: 99%

Proteomics analysis of Listeria monocytogenes ATCC 19115 in response to simultaneous triple stresses

Deng

Chen

et al. 2015

Arch Microbiol

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Listeria monocytogenes can cause listeriosis in humans through consumption of contaminated food. L. monocytogenes can adapt and grow in a vast array of physiochemical stresses in the food production environment. In this study, we performed a proteomics strategy in order to investigate how L. monocytogenes survives with a simultaneous exposure to low pH, high salinity and low temperature. The results showed that the adaptation processes mainly affected the biochemical pathways related to protein synthesis, oxidative stress, cell wall and nucleotide metabolism. Interestingly, enzymes involved in the carbohydrate metabolism of energy, such as glycolysis and pentose phosphate pathway, were derepressed due to the down-regulation of CodY, a global transcriptional repressor. The down-regulation of CodY, together with the up-regulation of carbohydrate metabolism enzymes, likely leads to the accumulation of pyruvate and further to the activation of fatty acid synthesis pathway. Proteomics profiling offered a better understanding of the physiological responses of this pathogen to adapt to harsh environment and would hopefully contribute to improving the food-processing and storage methods.

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“…There are also mitosomes (Tovar et al. 1999), which are organelles that have completely lost a genome and the ability to produce ATP but retain essential aspects of sulphur metabolism (Ali and Nozaki 2013). Organelles also exist that have characteristics intermediate between those of textbook mitochondria and hydrogenosomes (Stechmann et al.…”

Section: Introductionmentioning

confidence: 99%

BlastocystisMitochondrial Genomes Appear to Show Multiple Independent Gains and Losses of Start and Stop Codons

et al. 2016

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Complete mitochondrion-related organelle (MRO) genomes of several subtypes (STs) of the unicellular stramenopile Blastocystis are presented. Complete conservation of gene content and synteny in gene order is observed across all MRO genomes, comprising 27 protein coding genes, 2 ribosomal RNA genes, and 16 transfer RNA (tRNA) genes. Despite the synteny, differences in the degree of overlap between genes were observed between subtypes and also between isolates within the same subtype. Other notable features include unusual base-pairing mismatches in the predicted secondary structures of some tRNAs. Intriguingly, the rps4 gene in some MRO genomes is missing a start codon and, based on phylogenetic relationships among STs, this loss has happened twice independently. One unidentified open reading frame (orf160) is present in all MRO genomes. However, with the exception of ST4 where the feature has been lost secondarily, orf160 contains variously one or two in-frame stop codons. The overall evidence suggests that both the orf160 and rps4 genes are functional in all STs, but how they are expressed remains unclear.

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Iron–Sulphur Clusters, Their Biosynthesis, and Biological Functions in Protozoan Parasites

Cited by 34 publications

References 344 publications

Evolution of the Cytosolic Iron-Sulfur Cluster Assembly Machinery in Blastocystis Species and Other Microbial Eukaryotes

Evolution of the Cytosolic Iron-Sulfur Cluster Assembly Machinery in Blastocystis Species and Other Microbial Eukaryotes

Proteomics analysis of Listeria monocytogenes ATCC 19115 in response to simultaneous triple stresses

BlastocystisMitochondrial Genomes Appear to Show Multiple Independent Gains and Losses of Start and Stop Codons

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