Functional Analysis of Novel F1 ATPase Subunit in Trypanosoma brucei

0488329 - BC 2018 RIV CZ eng O - Ostatní výsledky
Váchová, H. - Šubrtová, Karolína - Gahura, Ondřej - Panicucci, Brian - Zíková, Alena
Functional Analysis of Novel F1 ATPase Subunit in Trypanosoma brucei.
2015
Grant CEP: GA MŠMT LL1205
Institucionální podpora: RVO:60077344
Klíčová slova: functional analysis * ATPase * T. brucei
Obor OECD: Biochemistry and molecular biology
http://www.parazitologie.cz/protozoologie/Protodny2015/JPD_sbornik_2015.pdf

FoF1-ATP synthase is a splendid molecular machine that produces ATP in bacteria and eukaryotic organelles. This complex is composed of the catalytic F1 moiety and membrane-bound Fo moiety. The composition of the catalytic F1 ATPase is extremely conserved between eukaryotes and includes subunits. No additional subunits were ever assigned to this moiety in any of the studied model organisms. In a parasitic protist, Trypanosoma brucei, the FoF1 ATP synthase/ATPase, differs in its function and activity between the insect (procyclic form, PF) and the mammalian (bloodstream form, BF) life stages. In PF cells this complex contributes to the total ATP production by oxidative phosphorylation while in BF cells it maintains the mitochondrial membrane potential (m). In contrast to other eukaryotes, a novel euglenozoa-specific subunit (p18) was purified together with the T. brucei F1 ATPase. To investigate if this protein is a bona fide subunit of F1 ATPase, the p18 expression was knocked-down in PF and BF trypanosomes. Our data suggest that p18 is important for growth of PF cells and crucial for BF cells viability. This observation is in agreement with the proposed essential function of FoF1 ATPase in the BF cells. Importantly, the stability of the F1 moiety was strongly affected in both PF and BF RNAi induced cells suggesting that p18 subunit is criticial for F1 ATPase structural integrity. As expected, the m was increased in PF cells while significantly decreased in BF cells in the absence of p18. In conclusion, our data suggest that p18 is novel subunit of F1 ATPase and this proposition breaks the long-standing conception of the strict conservancy of the F1-ATPase complex in
eukaryotes.
Trvalý link: http://hdl.handle.net/11104/0282929