We report here the identification of the novel subunit of the mitochon
drial F1F0-ATPase from Saccharomyces cerevisiae, ATPase subunit e. Yea
st ATPase subunit e displays significant similarities in both amino ac
id sequence, properties (hydropathy and predicted coiled-coil structur
e) and orientation in the inner membrane,,vith previously identified m
ammalian ATPase subunit e proteins, Estimation of its native molecular
mass and ability to be co-immunoprecipitated with a subunit of the F-
1-ATPase, demonstrate that subunit e is a subunit of the F1F0-ATPase.
Stable expression of subunit e requires the presence of the mitochondr
ially encoded subunits of the F-0-ATPase, Subunit e had been previousl
y identified as Tim11 and was proposed to be involved in the process o
f sorting of proteins to the mitochondrial inner membrane. (C) 1997 Fe
deration of European Biochemical Societies.