Discussion
The F
oF
1-ATP synthase is a reversible nanomotor synthesizing
ATP in bacteria and eukaryotic mitochondria. The core catalytic F
1
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 F
1-ATPase is believed
to be strictly conserved throughout evolution [1],
however this notion is based on the established structures of F
oF
1-ATP synthase complexes of bacteria and model eukaryotes and may not reflect full
eukaryotic diversity. Several reports have indicated that the Euglenozoa
F
1-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
oF
1-ATP synthase in trypanosomes.
We also aim to identify the protease responsible.
[1]J.E. Walker, Biochem. Soc. Trans. 41
(2013)
[2]A. Zikova, et al , PLoS Pathog. 5 (2009)
[3]D. Speijer, et al , Mol. Biochem. Parasitol. 85 (1997)
[4]R.E. Nelson, et al , Mol. Biochem. Parasitol. 135 (2004)
[5]E. Perez, et al , Mitochondrion 19 (2014)
PDF supporting document