Redesigned and reversed: architectural and functional oddities of the trypanosomal ATP synthase
The result's identifiers
Result code in 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>
Alternative codes found
RIV/60077344:_____/21:00553200
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Redesigned and reversed: architectural and functional oddities of the trypanosomal ATP synthase
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Parasitology
ISSN
0031-1820
e-ISSN
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Volume of the periodical
148
Issue of the periodical within the volume
10
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
1151-1160
UT code for WoS article
000674635600007
EID of the result in the Scopus database
2-s2.0-85100738533