Versatility of peroxisomes: An evolving concept

Deb, Rachayeeta; Nagotu, Shirisha

doi:10.1016/j.tice.2017.03.002

Cited by 27 publications

(12 citation statements)

References 234 publications

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“…Peroxisomes are multifunctional single‐membrane organelles present in almost all eukaryotes and function in diverse metabolic processes such as β‐oxidation, the glyoxylate cycle, biosynthesis of secondary metabolites and cholesterol metabolism (Gabaldon, ; Kubo, ; Deb & Nagotu, ). In recent years, it has been shown that peroxisomal breakdown of fatty acids is crucial for virulence in several plant pathogenic fungi such as U. maydis and M .…”

Section: Introductionmentioning

confidence: 99%

Virulence function of the Ustilago maydis sterol carrier protein 2

et al. 2018

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The peroxisomal sterol carrier protein 2 (Scp2) of the biotrophic maize pathogen Ustilago maydis was detected in apoplastic fluid, suggesting that it might function as a secreted effector protein. Here we analyze the role of the scp2 gene during plant colonization. We used reverse genetics approaches to delete the scp2 gene, determined stress sensitivity and fatty acid utilization of mutants, demonstrated secretion of Scp2, used quantitative reverse transcription polymerase chain reaction for expression analysis and expressed GFP-Scp2 fusion proteins for protein localization. scp2 mutants were strongly attenuated in virulence and this defect manifested itself during penetration. Scp2 localized to peroxisomes and peroxisomal targeting was necessary for its virulence function. Deletion of scp2 in U. maydis interfered neither with growth nor with peroxisomal β-oxidation. Conventionally secreted Scp2 protein could not rescue the virulence defect. scp2 mutants displayed an altered localization of peroxisomes. Our results show a virulence function for Scp2 during penetration that is probably carried out by Scp2 in peroxisomes. We speculate that Scp2 affects the lipid composition of membranes and in this way ensures the even cellular distribution of peroxisomes.

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Section: Introductionmentioning

confidence: 99%

Virulence function of the Ustilago maydis sterol carrier protein 2

et al. 2018

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“…Besides their most prevalent functions in fatty acid degradation and cellular detoxification, peroxisomal metabolism can be extremely versatile ( Smith and Aitchison 2013 ; Gabaldon et al. 2016 ; Deb and Nagotu 2017 ). It seems that these genome-less, single membrane-bound, dynamic compartments can be individually adapted to specific cellular needs by integrating whole or partial biochemical pathways in a “reaction chamber” that is spatially separated from the remaining cellular processes.…”

Section: Introductionmentioning

confidence: 99%

Identification and localization of peroxisomal biogenesis proteins indicates the presence of peroxisomes in the cryptophyte Guillardia theta and other ‘chromalveolates’

Mix

Cenci

Heimerl

et al. 2018

Genome Biology and Evolution

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Peroxisomes are single-membrane-bound organelles with a huge metabolic versatility, including the degradation of fatty acids (β-oxidation) and the detoxification of reactive oxygen species as most conserved functions. Although peroxisomes seem to be present in the majority of investigated eukaryotes, where they are responsible for many eclectic and important spatially separated metabolic reactions, knowledge about their existence in the plethora of protists (eukaryotic microorganisms) is scarce. Here, we investigated genomic data of organisms containing complex plastids with red algal ancestry (so-called “chromalveolates”) for the presence of genes encoding peroxins—factors specific for the biogenesis, maintenance, and division of peroxisomes in eukaryotic cells. Our focus was on the cryptophyte Guillardia theta, a marine microalga, which possesses two phylogenetically different nuclei of host and endosymbiont origin, respectively, thus being of enormous evolutionary significance. Besides the identification of a complete set of peroxins in G. theta, we heterologously localized selected factors as GFP fusion proteins via confocal and electron microscopy in the model diatom Phaeodactylum tricornutum. Furthermore, we show that peroxins, and thus most likely peroxisomes, are present in haptophytes as well as eustigmatophytes, brown algae, and alveolates including dinoflagellates, chromerids, and noncoccidian apicomplexans. Our results indicate that diatoms are not the only “chromalveolate” group devoid of the PTS2 receptor Pex7, and thus a PTS2-dependent peroxisomal import pathway, which seems to be absent in haptophytes (Emiliania huxleyi) as well. Moreover, important aspects of peroxisomal biosynthesis and protein import in “chromalveolates”are highlighted.

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“…Their biogenesis and maintenance is conducted by a conserved set of proteins known as peroxins (Pex) ( Smith and Aitchison 2013 ). Peroxisomes are metabolically highly versatile, single membrane-bound organelles present in most eukaryotes ( Deb and Nagotu 2017 ). Although peroxisomes can vary drastically in enzymatic content and number between different species and among different cell types, their most conserved metabolic functions are degradation of fatty acids (β-oxidation) and detoxification of reactive oxygen species (ROS; Gabaldon 2010 ).…”

Section: Introductionmentioning

confidence: 99%

Genomic and Proteomic Evidence for the Presence of a Peroxisome in the Apicomplexan Parasite Toxoplasma gondii and Other Coccidia

Moog

Przyborski

Maier

2017

Genome Biology and Evolution

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Apicomplexans are successful parasites responsible for severe human diseases including malaria, toxoplasmosis, and cryptosporidiosis. For many years, it has been discussed whether these parasites are in possession of peroxisomes, highly variable eukaryotic organelles usually involved in fatty acid degradation and cellular detoxification. Conflicting experimental data has been published. With the age of genomics, ever more high quality apicomplexan genomes have become available, that now allow a new assessment of the dispute. Here, we provide bioinformatic evidence for the presence of peroxisomes in Toxoplasma gondii and other coccidians. For these organisms, we have identified a complete set of peroxins, probably responsible for peroxisome biogenesis, division, and protein import. Moreover, via a global screening for peroxisomal targeting signals, we were able to show that a complete set of fatty acid β-oxidation enzymes is equipped with either PTS1 or PTS2 sequences, most likely mediating transport of these factors to putative peroxisomes in all investigated Coccidia. Our results further imply a life cycle stage-specific presence of peroxisomes in T. gondii and suggest several independent losses of peroxisomes during the evolution of apicomplexan parasites.

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Versatility of peroxisomes: An evolving concept

Cited by 27 publications

References 234 publications

Virulence function of the Ustilago maydis sterol carrier protein 2

Virulence function of the Ustilago maydis sterol carrier protein 2

Identification and localization of peroxisomal biogenesis proteins indicates the presence of peroxisomes in the cryptophyte Guillardia theta and other ‘chromalveolates’

Genomic and Proteomic Evidence for the Presence of a Peroxisome in the Apicomplexan Parasite Toxoplasma gondii and Other Coccidia

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