Abstract: The ATP synthase of the yeast Saccharomyces cerevisiae is composed of 20 different subunits whose primary structure is known. The organization of proteins that constitute the membranous domain is now under investigation. Cysteine insertions combined with the use of nonpermeant maleimide reagents and cross-linking reagents showing different lengths and specificity contribute 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 summarizes data on yeast ATP synthase obtained in our laboratory since 1980.