FOF1-ATP synthase: When it pays to go in reverse

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F24%3A00604983" target="_blank" >RIV/60077344:_____/24:00604983 - isvavai.cz</a>

Výsledek na webu

<a href="https://doi.org/10.1016/j.bbabio.2024.149174" target="_blank" >https://doi.org/10.1016/j.bbabio.2024.149174</a>

DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

FOF1-ATP synthase: When it pays to go in reverse

Popis výsledku v původním jazyce

FoF1-ATP synthase is a reversible nanomachine that synthesizes or hydrolyzes ATP depending on the bioenergetic properties of the mitochondria. A perfect example of this dual functionality is found in the mammalian pathogen Trypanosoma brucei. During the switch between the mammalian and insect host, the activity of ATP synthase also changes. In the mammalian host bloodstream, abundant glucose allows the parasite to fully utilize its aerobic glycolysis, which is linked to respiration via the alternative oxidase, and in the absence of complexes III and IV of the electron transport chain (ETC), the mitochondrial membrane potential is maintained by the reverse activity of ATP synthase. In contrast, the parasite in the midgut of the insect vector, tsetse fly, consumes abundant amino acids and utilizes a fully developed cytochrome-containing ETC and ATP synthase to generate ATP by oxidative phosphorylation. Expression of the ATP synthase inhibitory peptide IF1 fluctuates as it is absent in the bloodstream form (BF) parasites and abundant in the procyclic form (PF) inhabiting the tsetse midgut. Therefore, the regulation of IF1 gene expression appears to be crucial for the correct developmental progression of the parasite.n

Název v anglickém jazyce

FOF1-ATP synthase: When it pays to go in reverse

Popis výsledku anglicky

FoF1-ATP synthase is a reversible nanomachine that synthesizes or hydrolyzes ATP depending on the bioenergetic properties of the mitochondria. A perfect example of this dual functionality is found in the mammalian pathogen Trypanosoma brucei. During the switch between the mammalian and insect host, the activity of ATP synthase also changes. In the mammalian host bloodstream, abundant glucose allows the parasite to fully utilize its aerobic glycolysis, which is linked to respiration via the alternative oxidase, and in the absence of complexes III and IV of the electron transport chain (ETC), the mitochondrial membrane potential is maintained by the reverse activity of ATP synthase. In contrast, the parasite in the midgut of the insect vector, tsetse fly, consumes abundant amino acids and utilizes a fully developed cytochrome-containing ETC and ATP synthase to generate ATP by oxidative phosphorylation. Expression of the ATP synthase inhibitory peptide IF1 fluctuates as it is absent in the bloodstream form (BF) parasites and abundant in the procyclic form (PF) inhabiting the tsetse midgut. Therefore, the regulation of IF1 gene expression appears to be crucial for the correct developmental progression of the parasite.n

Druh

O - Ostatní výsledky

CEP obor

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OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

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Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2024

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů