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.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D007700:Kinetics; D046911:Macromolecular Substances; D008928:Mitochondria / Q000201:enzymology*; D010086:Oxidative Phosphorylation Coupling Factors / Q000378:metabolism; D010446:Peptide Fragments / Q000032:analysis; D006180:Proton-Translocating ATPases; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D014357:Trypsin
D046911:Macromolecular Substances; D010086:Oxidative Phosphorylation Coupling Factors; D010446:Peptide Fragments; D014357:Trypsin; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases