Authors

K Subrtova¹; O Gahura²; M Saldivia³; B Panicucci²; J Mottram³; A Zikova²; A Schnaufer¹;  ¹ Institute of Immunology and Infection Research, University of Edinburgh;  ² Institute of Parasitology, Biology Centre, ASCR, Czech Republic;  ³ University of York, Centre for Immunology and Infection

Discussion

The F_oF₁-ATP synthase is a reversible nanomotor synthesizing ATP in bacteria and eukaryotic mitochondria. The core catalytic F₁ moiety of this multisubunit complex is formed by a globular hexamer of alternating subunits α and β sitting on a central stalk consisting of subunit γ and small subunits δ and ε [1]. The composition and structure of the core F₁-ATPase is believed to be strictly conserved throughout evolution [1], however this notion is based on the established structures of F_oF₁-ATP synthase complexes of bacteria and model eukaryotes and may not reflect full eukaryotic diversity. Several reports have indicated that the Euglenozoa F₁-ATPase subunit a is split into two fragments, presumably by proteolytic cleavage [2-5]. Both fragments stay associated with the complex. This feature appears to have no parallel in any other group of organisms. In this project, we are investigating whether a cleavage results in novel features of this key enzyme, that are important for the structure/function of F_oF₁-ATP synthase in trypanosomes. We also aim to identify the protease responsible.