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  • 1
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    Localization and functionality of microsporidian iron-sulphur cluster assembly proteins (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-03-04
    Description: Microsporidia are highly specialized obligate intracellular parasites of other eukaryotes (including humans) that show extreme reduction at the molecular, cellular and biochemical level. Although microsporidia have long been considered as early branching eukaryotes that lack mitochondria, they have recently been shown to contain a tiny mitochondrial remnant called a mitosome. The function of the mitosome is unknown, because microsporidians lack the genes for canonical mitochondrial functions, such as aerobic respiration and haem biosynthesis. However, microsporidial genomes encode several components of the mitochondrial iron-sulphur (Fe-S) cluster assembly machinery. Here we provide experimental insights into the metabolic function and localization of these proteins. We cloned, functionally characterized and localized homologues of several central mitochondrial Fe-S cluster assembly components for the microsporidians Encephalitozoon cuniculi and Trachipleistophora hominis. Several microsporidial proteins can functionally replace their yeast counterparts in Fe-S protein biogenesis. In E. cuniculi, the iron (frataxin) and sulphur (cysteine desulphurase, Nfs1) donors and the scaffold protein (Isu1) co-localize with mitochondrial Hsp70 to the mitosome, consistent with it being the functional site for Fe-S cluster biosynthesis. In T. hominis, mitochondrial Hsp70 and the essential sulphur donor (Nfs1) are still in the mitosome, but surprisingly the main pools of Isu1 and frataxin are cytosolic, creating a conundrum of how these key components of Fe-S cluster biosynthesis coordinate their function. Together, our studies identify the essential biosynthetic process of Fe-S protein assembly as a key function of microsporidian mitosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldberg, Alina V -- Molik, Sabine -- Tsaousis, Anastasios D -- Neumann, Karina -- Kuhnke, Grit -- Delbac, Frederic -- Vivares, Christian P -- Hirt, Robert P -- Lill, Roland -- Embley, T Martin -- England -- Nature. 2008 Apr 3;452(7187):624-8. doi: 10.1038/nature06606. Epub 2008 Mar 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Cell and Molecular Biosciences, The Catherine Cookson Building, Newcastle University, Newcastle upon Tyne NE2 4HH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18311129" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cloning, Molecular ; Fungal Proteins/genetics/*metabolism ; HSP70 Heat-Shock Proteins/genetics/metabolism ; Iron-Binding Proteins/genetics/metabolism ; Iron-Sulfur Proteins/*biosynthesis/genetics/metabolism ; Microsporidia/cytology/genetics/*metabolism ; Mitochondria/metabolism ; Molecular Sequence Data ; Protein Transport ; Rabbits ; Saccharomyces cerevisiae/cytology/genetics/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
    Electronic Resource
    Electronic Resource
    Preservation of ptp1 and ptp2 Gene Synteny in Two Microsporidia Parasite of Insects: Nosema locustae and Nosema grylli (2005)
    Oxford, UK : Blackwell Science Inc
    The @journal of eukaryotic microbiology 52 (2005), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Microsporidia are obligate intracellular parasites infecting a wide range of invertebrate and vertebrate hosts including human. The spore contains a specialized organelle called the polar tube involved in host cell invasion. Three polar tube proteins (PTP1-3) have been identified in Encephalitozoon cuniculi. The genes coding for ptp1 and ptp2 are localized on the same chromosome and are at a distance of 860 bp. A similar synteny organization is found in two other Encephalitozoon species. Comparison of the E. cuniculi genome with that of Nosema locustae, an microsporidia parasite of grasshoppers, indicates that several genes are positioned in the same order and orientation. This allowed the identification of two ORFs distant of 1117 bp, that despite divergent sequence features, encode proteins having common characteristics with Encephalitozoon PTP1 and PTP2 (signal peptide, proline-rich internal repeats for PTP1, lysine-rich protein for PTP2 …). To test whether they correspond to PTP, polyclonal sera were raised against two recombinant proteins expressed in E. coli. In indirect immunofluorescence, the extruded polar tubes of N. locustae spores are specifically labelled. NlPTP1 and NlPTP2 have 355 and 287 amino acids, respectively, and are only soluble in the presence of high concentrations of reducing agent.Aptp1 and ptp2 containing cluster have been also identified in Nosema grylli. PTP1 from N. locustae and N. grylli present a strong variability in the proline-rich internal repeats, whilst PTP2s are highly conserved. It would be interesting to show whether this gene synteny conservation is related to a specific interaction between PTP1 and PTP2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.2005.05202003_3_21.x
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  • 3
    Electronic Resource
    Electronic Resource
    Identification of Sporal Proteins in Two Microsporidian Species: An Immunoblotting and Immunocytochemical Study (1996)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 43 (1996), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.1996.tb05024.x
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  • 4
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    Fate and ecotoxicological impact of new generation herbicides from the triketone family: An overview to assess the environmental risks (2017)
    Elsevier
    Details
    Publication Date: 2017-03-01
    Print ISSN: 0304-3894
    Electronic ISSN: 1873-3336
    Topics: Chemistry and Pharmacology , Energy, Environment Protection, Nuclear Power Engineering , Technology
    Published by Elsevier
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