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Comparative Metabolism of Free-living Bodo saltans and Parasitic Trypanosomatids

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    0469001 - BC 2017 RIV US eng J - Journal Article
    Opperdoes, F. R. - Butenko, A. - Flegontov, P. - Yurchenko, V. - Lukeš, Julius
    Comparative Metabolism of Free-living Bodo saltans and Parasitic Trypanosomatids.
    Journal of Eukaryotic Microbiology. Roč. 63, č. 5 (2016), s. 657-678. ISSN 1066-5234. E-ISSN 1550-7408
    R&D Projects: GA ČR(CZ) GA14-23986S
    Grant - others:EU COST Action CM1307
    Institutional support: RVO:60077344
    Keywords : adaptation * Leishmania * Leptomonas * lateral gene transfer * parasitism * Phytomonas * Trypanosoma
    Subject RIV: EB - Genetics ; Molecular Biology
    Impact factor: 2.692, year: 2016

    Comparison of the genomes of free-living Bodo saltans and those of parasitic trypanosomatids reveals that the transition from a free-living to a parasitic life style has resulted in the loss of approximately 50% of protein-coding genes. Despite this dramatic reduction in genome size, B. saltans and trypanosomatids still share a significant number of common metabolic traits: glycosomes; a unique set of the pyrimidine biosynthetic pathway genes; an ATP-PFK which is homologous to the bacterial PPi-PFKs rather than to the canonical eukaryotic ATP-PFKs; an alternative oxidase; three phosphoglycerate kinases and two GAPDH isoenzymes; a pyruvate kinase regulated by fructose-2,6-bisphosphate; trypanothione as a substitute for glutathione; synthesis of fatty acids via a unique set of elongase enzymes; and a mitochondrial acetate: succinate coenzyme A transferase. B. saltans has lost the capacity to synthesize ubiquinone. Among genes that are present in B. saltans and lost in all trypanosomatids are those involved in the degradation of mureine, tryptophan and lysine. Novel acquisitions of trypanosomatids are components of pentose sugar metabolism, pteridine reductase and bromodomain-factor proteins. In addition, only the subfamily Leishmaniinae has acquired a gene for catalase and the capacity to convert diaminopimelic acid to lysine.
    Permanent Link: http://hdl.handle.net/11104/0266908

     
     
Number of the records: 1  

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