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Redesigned and reversed: architectural and functional oddities of the trypanosomal ATP synthase
O. Gahura, C. Hierro-Yap, A. Zíková
Jazyk angličtina Země Velká Británie
Typ dokumentu časopisecké články, práce podpořená grantem, přehledy
NLK
PubMed Central
od 2020
ProQuest Central
od 2001-01-01 do Před 1 rokem
Health & Medicine (ProQuest)
od 2001-01-01 do Před 1 rokem
Public Health Database (ProQuest)
od 2001-01-01 do Před 1 rokem
ROAD: Directory of Open Access Scholarly Resources
od 1908
- MeSH
- genetické inženýrství * MeSH
- Leishmania enzymologie MeSH
- membránový potenciál mitochondrií MeSH
- mitochondriální protonové ATPasy genetika metabolismus MeSH
- protozoální proteiny genetika metabolismus MeSH
- Trypanosoma brucei brucei enzymologie MeSH
- Trypanosoma cruzi enzymologie MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- přehledy MeSH
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.
Biology Centre Czech Academy of Sciences Branišovská 31 České Budějovice 37005 Czech Republic
Faculty of Science University of South Bohemia Branišovská 31 České Budějovice 37005 Czech Republic
Citace poskytuje Crossref.org
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