Structure of the yeast mitochondrial adenosine triphosphatase. Results of trypsin degradation.

A comparison was made of the subunit sensitivities of the F1-ATPase and the Triton-solubilized ATPase complex to trypsin degradation. The dissociation of the F1-ATPase from ATPase complex increased the trypsin sensitivity of subunit 3 by a factor of 2 and increased the sensitivity of a particular trypsin site (or group of sites) on subunit 1 by 7-fold. The overall degradation of subunits 1 and 2 appears to be the same in solubilized ATPase complex and the F1-ATPase. Implications of these findings for structural models of the ATPase complex are discussed.