Jean Velours

TL;DR: A model is proposed of the assembly of ATP synthase dimers, taking into account the oligomerization of the yeast enzyme and earlier data on the ultrastructure of mitochondrial cristae, which suggests that the association of mitochondria of yeast cells deficient in either subunits e or g is involved in the control of the biogenesis of the inner mitochondrial membrane.

TL;DR: The findings imply that an intact F0F1-ATPase in the inner membrane of mitochondria is necessary for optimal function of Bax in both yeast and mammalian cells.

TL;DR: The data demonstrate that the inner structure of mitochondria depends upon the ability of ATP synthase to make supramolecular structures, which is fully reversible upon removal of doxycycline.

TL;DR: The data show the involvement of the dimerization motif of subunit e in the formation of supramolecular structures of mitochondrial ATP synthases and are in favour of the existence in the inner mitochondrial membrane of associations of ATP synthase whose masses are higher than those of ATP synthesis dimers.

TL;DR: Western blot analysis showed that Fmc1p is a soluble protein located in the mitochondrial matrix that is required for the proper folding/stability or functioning of Atp12p in heat stress conditions.