Počet záznamů: 1  

Role of OSCP protein in bloodstream form and dyskinetoplastic Trypanosoma brucei

  1. 1.
    SYSNO ASEP0488333
    Druh ASEPO - Ostatní výsledky
    Zařazení RIVO - Ostatní
    NázevRole of OSCP protein in bloodstream form and dyskinetoplastic Trypanosoma brucei
    Tvůrce(i) Hierro Yap, C. (CZ)
    Gahura, Ondřej (BC-A) RID, ORCID
    Panicucci, Brian (BC-A)
    Zíková, Alena (BC-A) RID, ORCID
    Rok vydání2016
    Jazyk dok.eng - angličtina
    Země vyd.CZ - Česká republika
    Klíč. slovaOSCP ; bloodstream ; T. brucei
    Vědní obor RIVEB - Genetika a molekulární biologie
    Obor OECDBiochemistry and molecular biology
    CEPLL1205 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy
    Institucionální podporaBC-A - RVO:60077344
    AnotaceMitochondrial (mt) ATP synthase is responsible of ATP generation in most eukaryotic cells. While the procyclic form (PF) of T. brucei uses the conventional function of the enzyme, the bloodstream form (BF) exploits the reversed ATP hydrolytic activity coupled to the proton translocation across the inner mt membrane in order to maintain the mt membrane potential. Despite ATP synthase overall structure and mechanism have remained conserved throughout evolution, composition of T. brucei's peripheral stalk, which docks 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 subunit. However, critical residues for the interaction are found neither in OSCP nor in subunit. Consequently, OSCP role in F1-ATPase immobilization remains hypothetical in T. brucei. OSCP is required for ATP synthase function in PF, as its silencing by RNAi resulted in an evident growth phenotype. In contrast, OSCP knock-down in BF or dyskinetoplastic (Dk) cell lines did not affect growth rate. ATP synthase of Dk cells cannot translocate protons due to the loss of the mt encoded proton pore subunit a. Nevertheless, ATP hydrolysis by F1-ATPase remains essential for by supplying ADP3-/ATP4-exchange across the mt membrane. OSCP double knockout in BF and in Dk cell lines will enable us to determine whether the F1-peripheral stalk interaction is OSCP-mediated, or involves other subunits, e.g. kinetoplastid-specific ATPaseTb2 (peripheral stalk) or p18 (F1 sector), and whether the interaction network is preserved in the reduced ATP synthase of Dk cells.
    PracovištěBiologické centrum (od r. 2006)
    KontaktDana Hypšová, eje@eje.cz, Tel.: 387 775 214
    Rok sběru2018
    Elektronická adresahttp://www.parazitologie.cz/protozoologie/Protodny2016/JPD_sbornik_2016.pdf
Počet záznamů: 1  

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