Adenosine triphosphatase yeast

Kane, P. M., Yamashiro, C. T., Wolczyk, D. F., Neff, N., Goebl, M., and Stevens, T. H. (1990). Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H (+)-adenosine triphosphatase. Science 250, 651-657. 

The primary antimicrobial form of SO2 is molecular or unionised SO2, followed by bisulphite and sulphite forms, which have minimal antimicrobial activity (Ough et al, 1983). The undissociated, molecular form penetrates the yeast cell membrane by diffusion and subsequently inactivates intracellular constituents (Schmiz, 1980 Stratford and Rose, 1986). In the cell, SO2 activates ATPase (adenosine triphosphatase), the ATP-hydrolysing enzyme, causing a decrease in the concentration of ATP furthermore, once the SO2 has entered the yeast cell, it dissociates, in response to the difference between the pH of grape juice and that of the cell, and becomes trapped. The bisulphite and sulphite ions then react with the cellular constituents. The combined effects of ATP depletion and cellular activity lead to inactivation and eventual death of the cell (Schmiz and Holzer, 1977 Beech and Thomas, 1985 Stratford and Rose, 1986). 

Some of the yeast membrane proteins have been studied in greater depth. These include adenosine triphosphatase (ATPase), solute (sugars and amino... 

Kane PM et al (1990) Protein splicing converts the yeast TFPl gene product to the 69-kD subimit of the vacuolar H(-i)-adenosine triphosphatase. Science 250 651-657... 

Ohta S, Tsuboi M, Yoshida M and Kagawa Y (1980) Inter subunit interaction in proton translocating adenosine triphosphatase as revealed by hydrogen exchange kinetics. Biochemistry 19t 2160-2164. Pullman ME and Monroy GC (1963) A naturally occuring inhibitor of mitochondrial adenosine triphosphtase, J. Biol. Chem. 238, 3762-3769. Rott R and Nelson N (1981) Purification and immunological properties of proton ATPase complexes from yeast and rat liver mitochondria, J. Biol. Chem. 256, 9224-9228. 

Tod RD and Douglas MG (1981) A model for the structure of the yeast mitochondrial adenosine triphosphatase complex, J. Biol. Chem. 256, 6984-6989. 

Schatz G, Penefsky HS, Racker E (1967) Partial resolution of the enzymes catalyzing oxidative phosphorylation XIV Interaction of purified mitochondrial adenosine triphosphatase from Bakers yeast with submitochondrial particles from beef heart. J. Biol. Chem. 242,2552-2560... 

The proteins of membranes often include enzymes, e.g. adenosine triphosphatase which occurs in the plasma membrane of yeast where it assists uptake of aminoacids (Post et aL i960) and permeases (Section 2.1) are commonly found in membranes. It is logical to suppose that the protruding parts of the membrane proteins are made mainly of aminoacids with polar side-chains, whereas the embedded parts are rich in aminoacids with non-polar side-chains. 

---