The ATP synthase of the yeast Saccharomyces cerevisiae is composed of 20 di
fferent subunits whose primary structure is known. The organization of prot
eins that constitute the membranous domain is now under investigation. Cyst
eine insertions combined with the use of nonpermeant maleimide reagents and
cross-linking reagents showing different lengths and specificity contribut
e to the knowledge of the location of the N- and C-termini of the subunits
involved in the stator of the enzyme and their organization. This review su
mmarizes data on yeast ATP synthase obtained in our laboratory since 1980.