Redesigned and reversed: architectural and functional oddities of the trypanosomal ATP synthase
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F21%3A43903337" target="_blank" >RIV/60076658:12310/21:43903337 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/60077344:_____/21:00553200
Výsledek na webu
<a href="https://www.cambridge.org/core/journals/parasitology/article/redesigned-and-reversed-architectural-and-functional-oddities-of-the-trypanosomal-atp-synthase/706AEA73FAB6B53628E5460DFCA02B83" target="_blank" >https://www.cambridge.org/core/journals/parasitology/article/redesigned-and-reversed-architectural-and-functional-oddities-of-the-trypanosomal-atp-synthase/706AEA73FAB6B53628E5460DFCA02B83</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1017/S0031182021000202" target="_blank" >10.1017/S0031182021000202</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Redesigned and reversed: architectural and functional oddities of the trypanosomal ATP synthase
Popis výsledku v původním jazyce
Mitochondrial F-type adenosine triphosphate (ATP) synthases are commonly introduced as highly conserved membrane-embedded rotary machines generating the majority of cellular ATP. This simplified view neglects recently revealed striking compositional diversity of the enzyme and the fact that in specific life stages of some parasites, the physiological role of the enzyme is to maintain the mitochondrial membrane potential at the expense of ATP rather than to produce ATP. In addition, mitochondrial ATP synthases contribute indirectly to the organelle's other functions because they belong to major determinants of submitochondrial morphology. Here, we review current knowledge about the trypanosomal ATP synthase composition and architecture in the context of recent advances in the structural characterization of counterpart enzymes from several eukaryotic supergroups. We also discuss the physiological function of mitochondrial ATP synthases in three trypanosomatid parasites, Trypanosoma cruzi, Trypanosoma brucei and Leishmania, with a focus on their disease-causing life cycle stages. We highlight the reversed proton-pumping role of the ATP synthase in the T. brucei bloodstream form, the enzyme's potential link to the regulation of parasite's glycolysis and its role in generating mitochondrial membrane potential in the absence of mitochondrial DNA.
Název v anglickém jazyce
Redesigned and reversed: architectural and functional oddities of the trypanosomal ATP synthase
Popis výsledku anglicky
Mitochondrial F-type adenosine triphosphate (ATP) synthases are commonly introduced as highly conserved membrane-embedded rotary machines generating the majority of cellular ATP. This simplified view neglects recently revealed striking compositional diversity of the enzyme and the fact that in specific life stages of some parasites, the physiological role of the enzyme is to maintain the mitochondrial membrane potential at the expense of ATP rather than to produce ATP. In addition, mitochondrial ATP synthases contribute indirectly to the organelle's other functions because they belong to major determinants of submitochondrial morphology. Here, we review current knowledge about the trypanosomal ATP synthase composition and architecture in the context of recent advances in the structural characterization of counterpart enzymes from several eukaryotic supergroups. We also discuss the physiological function of mitochondrial ATP synthases in three trypanosomatid parasites, Trypanosoma cruzi, Trypanosoma brucei and Leishmania, with a focus on their disease-causing life cycle stages. We highlight the reversed proton-pumping role of the ATP synthase in the T. brucei bloodstream form, the enzyme's potential link to the regulation of parasite's glycolysis and its role in generating mitochondrial membrane potential in the absence of mitochondrial DNA.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10608 - Biochemistry and molecular biology
Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2021
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Parasitology
ISSN
0031-1820
e-ISSN
—
Svazek periodika
148
Číslo periodika v rámci svazku
10
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
10
Strana od-do
1151-1160
Kód UT WoS článku
000674635600007
EID výsledku v databázi Scopus
2-s2.0-85100738533