Function of OSCP protein in the peripheral stalk of the versatile mitochondrial ATP synthase in Trypanosoma brucei

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F17%3A00488339" target="_blank" >RIV/60077344:_____/17:00488339 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Function of OSCP protein in the peripheral stalk of the versatile mitochondrial ATP synthase in Trypanosoma brucei

Popis výsledku v původním jazyce

Mitochondrial (mt) ATP synthase is responsible of ATP generation in most eukaryotic cells. In Trypanosoma brucei it constitutes a very versatile enzyme since its function varies depending on the parasite’s life cycle stage. The procyclic form (PF) utilises the enzyme to carry out the so-called oxidative phosphorylation, where ATP synthesis is driven by a proton flow across the inner mt membrane. Conversely, the bloodstream form (BF) exploits the reverse function of the enzyme, hydrolysing ATP in order to maintain the essential mt membrane potential. Although mt ATP synthase overall structure and mechanism have been tightly conserved throughout evolution, the enzymes from various organisms differ in subunit composition and/or sequence, as well as in the mechanisms for catalytic activity regulation. The composition of T. brucei’s peripheral stalk, which docks the F1 moiety to the membrane, differs remarkably, being OSCP the only conserved subunit thereof. In other species, OSCP constitutes the only physical link of the peripheral stalk to F1-ATPase via an interaction with α subunit. However, critical residues for the interaction are found neither in OSCP nor in α subunit. Consequently, OSCP role in F1-ATPase immobilization remains hypothetical in T. brucei.n

Název v anglickém jazyce

Function of OSCP protein in the peripheral stalk of the versatile mitochondrial ATP synthase in Trypanosoma brucei

Popis výsledku anglicky

Mitochondrial (mt) ATP synthase is responsible of ATP generation in most eukaryotic cells. In Trypanosoma brucei it constitutes a very versatile enzyme since its function varies depending on the parasite’s life cycle stage. The procyclic form (PF) utilises the enzyme to carry out the so-called oxidative phosphorylation, where ATP synthesis is driven by a proton flow across the inner mt membrane. Conversely, the bloodstream form (BF) exploits the reverse function of the enzyme, hydrolysing ATP in order to maintain the essential mt membrane potential. Although mt ATP synthase overall structure and mechanism have been tightly conserved throughout evolution, the enzymes from various organisms differ in subunit composition and/or sequence, as well as in the mechanisms for catalytic activity regulation. The composition of T. brucei’s peripheral stalk, which docks the F1 moiety to the membrane, differs remarkably, being OSCP the only conserved subunit thereof. In other species, OSCP constitutes the only physical link of the peripheral stalk to F1-ATPase via an interaction with α subunit. However, critical residues for the interaction are found neither in OSCP nor in α subunit. Consequently, OSCP role in F1-ATPase immobilization remains hypothetical in T. brucei.n

Druh

O - Ostatní výsledky

CEP obor

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OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/LL1205" target="_blank" >LL1205: Charakterizace unikátních vlastností esenciální FoF1 ATP syntázy u původce africké spavé nemoci Trypanosoma bucei za účelem vývoje inhibitorů tohoto komplexu.</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2017

Kód důvěrnosti údajů

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