Comparative Metabolism of Free-living Bodo saltans and Parasitic Trypanosomatids

0469001 - BC 2017 RIV US eng J - Článek v odborném periodiku
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
Grant CEP: GA ČR(CZ) GA14-23986S
Grant ostatní: EU COST Action CM1307
Institucionální podpora: RVO:60077344
Klíčová slova: adaptation * Leishmania * Leptomonas * lateral gene transfer * parasitism * Phytomonas * Trypanosoma
Kód oboru RIV: EB - Genetika a molekulární biologie
Impakt faktor: 2.692, rok: 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.
Trvalý link: http://hdl.handle.net/11104/0266908