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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
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    A novel route for ATP acquisition by the remnant mitochondria of Encephalitozoon cuniculi (2008)
    Nature Publishing Group (NPG)
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    Publication Date: 2008-05-02
    Description: Mitochondria use transport proteins of the eukaryotic mitochondrial carrier family (MCF) to mediate the exchange of diverse substrates, including ATP, with the host cell cytosol. According to classical endosymbiosis theory, insertion of a host-nuclear-encoded MCF transporter into the protomitochondrion was the key step that allowed the host cell to harvest ATP from the enslaved endosymbiont. Notably the genome of the microsporidian Encephalitozoon cuniculi has lost all of its genes for MCF proteins. This raises the question of how the recently discovered microsporidian remnant mitochondrion, called a mitosome, acquires ATP to support protein import and other predicted ATP-dependent activities. The E. cuniculi genome does contain four genes for an unrelated type of nucleotide transporter used by plastids and bacterial intracellular parasites, such as Rickettsia and Chlamydia, to import ATP from the cytosol of their eukaryotic host cells. The inference is that E. cuniculi also uses these proteins to steal ATP from its eukaryotic host to sustain its lifestyle as an obligate intracellular parasite. Here we show that, consistent with this hypothesis, all four E. cuniculi transporters can transport ATP, and three of them are expressed on the surface of the parasite when it is living inside host cells. The fourth transporter co-locates with mitochondrial Hsp70 to the E. cuniculi mitosome. Thus, uniquely among eukaryotes, the traditional relationship between mitochondrion and host has been subverted in E. cuniculi, by reductive evolution and analogous gene replacement. Instead of the mitosome providing the parasite cytosol with ATP, the parasite cytosol now seems to provide ATP for the organelle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsaousis, Anastasios D -- Kunji, Edmund R S -- Goldberg, Alina V -- Lucocq, John M -- Hirt, Robert P -- Embley, T Martin -- MC_U105663139/Medical Research Council/United Kingdom -- Medical Research Council/United Kingdom -- England -- Nature. 2008 May 22;453(7194):553-6. doi: 10.1038/nature06903. Epub 2008 Apr 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Cell and Molecular Biosciences, Catherine Cookson Building, Framlington Place, 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/18449191" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/*metabolism ; Animals ; Biological Transport ; Carrier Proteins/genetics/immunology/metabolism ; Cell Line ; Encephalitozoon cuniculi/*cytology/genetics/*metabolism ; Escherichia coli/genetics/metabolism ; Fungal Proteins/genetics/immunology/metabolism ; Genome, Fungal/genetics ; Genome, Mitochondrial/genetics ; Mitochondria/genetics/*metabolism ; Models, Biological ; Molecular Sequence Data ; Rabbits ; Rats ; Symbiosis
    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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  • 3
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    Transporter gene acquisition and innovation in the evolution of Microsporidia intracellular parasites (2018)
    Springer Nature
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    Publication Date: 2018-04-28
    Description: Transporter gene acquisition and innovation in the evolution of Microsporidia intracellular parasites Transporter gene acquisition and innovation in the evolution of Microsporidia intracellular parasites, Published online: 27 April 2018; doi:10.1038/s41467-018-03923-4 Microsporidia are obligate intracellular parasites that infect both humans and animals. Here, Dean et al. perform ancient gene reconstruction and functional assays to investigate the evolution and functional diversification of nucleotide transporters which are key to the parasite's intracellular lifestyle.
    Electronic ISSN: 2041-1723
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General , Physics
    Published by Springer Nature
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  • 4
    Electronic Resource
    Electronic Resource
    On Implementing the Push—Relabel Method for the Maximum Flow Problem (1997)
    Springer
    Algorithmica 19 (1997), S. 390-410 
    Details
    ISSN: 1432-0541
    Keywords: Key words. Algorithms, Network optimization, Maximum flows, Experimental evaluation.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Computer Science , Mathematics
    Notes: Abstract. We study efficient implementations of the push—relabel method for the maximum flow problem. The resulting codes are faster than the previous codes, and much faster on some problem families. The speedup is due to the combination of heuristics used in our implementations: we show that the highest-level selection strategy gives better results when combined with both global and gap relabeling heuristics. We also exhibit a family of problems for which the running time of all implementations we consider is quadratic.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00009180
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  • 5
    Electronic Resource
    Electronic Resource
    Program to calculate the structural and energetic properties of aqueous solutions of binary systems using the Monte Carlo method (1990)
    Springer
    Journal of structural chemistry 31 (1990), S. 686-686 
    Details
    ISSN: 1573-8779
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00752509
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  • 6
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    On Implementing the Push—Relabel Method for the Maximum Flow Problem (1997)
    Springer
    Details
    Publication Date: 1997-12-01
    Print ISSN: 0178-4617
    Electronic ISSN: 1432-0541
    Topics: Computer Science , Mathematics
    Published by Springer
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  • 7
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    Phosphorylation of Rpn6/PSMD11 by PKA [Biochemistry] (2015)
    National Academy of Sciences
    Details
    Publication Date: 2015-12-30
    Description: Although rates of protein degradation by the ubiquitin-proteasome pathway (UPS) are determined by their rates of ubiquitination, we show here that the proteasome’s capacity to degrade ubiquitinated proteins is also tightly regulated. We studied the effects of cAMP-dependent protein kinase (PKA) on proteolysis by the UPS in several mammalian cell...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 8
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    Transporter gene acquisition and innovation in the evolution of Microsporidia intracellular parasites (2018)
    Springer Nature
    Details
    Publication Date: 2018-04-27
    Electronic ISSN: 2041-1723
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General , Physics
    Published by Springer Nature
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