scholarly journals Characterization of Plasma Membrane ATPase and Mitochondrial ATPase in Relation to the Salt-tolerance in Zygosaccharomyces rouxii

1991 ◽  
Vol 86 (5) ◽  
pp. 365-371 ◽  
Author(s):  
Kohei USHIO ◽  
Harumi OTSUKA ◽  
Yoshiyuki NAKATA
1997 ◽  
Vol 43 (7) ◽  
pp. 683-687 ◽  
Author(s):  
Alexandra Veiga ◽  
Ana Ferreira Pinto ◽  
Maria C. Loureiro-Dias

Rhodotorula ferulica, a yeast able to utilize phenolic compounds, was chosen for evaluating the effects of tributyltin oxide (TBTO) on this utilization. TBTO reduced respiratory capacity when vanillic or benzoic acid was the energy source. The ATP level of the cells was severely affected by 2 μM TBTO. The mitochondrial ATPase was strongly inhibited by 0.5 μM TBTO, whereas the activity of the plasma membrane ATPase was not affected by concentrations of TBTO up to 30 μM. Our data support the hypothesis that the target for TBTO action is the mitochondrial ATPase, resulting in a severe disturbance of the yeast utilization of aromatic compounds.Key words: TBTO, tributyltin, yeast, Rhodotorula ferulica, respiration, ATPase.


1988 ◽  
Vol 106 (3) ◽  
pp. 641-648 ◽  
Author(s):  
C L Holcomb ◽  
W J Hansen ◽  
T Etcheverry ◽  
R Schekman

Yeast cell surface growth is accomplished by constitutive secretion and plasma membrane assembly, culminating in the fusion of vesicles with the bud membrane. Coordination of secretion and membrane assembly has been investigated by examining the biogenesis of plasma membrane ATPase (PM ATPase) in secretion-defective (sec) strains of Saccharomyces cerevisiae. PM ATPase is synthesized as a approximately 106-kD polypeptide that is not detectably modified by asparagine-linked glycosylation or proteolysis during transit to the plasma membrane. Export of the PM ATPase requires the secretory pathway. In sec1, a mutant defective in the last step of secretion, large amounts of Golgi-derived vesicles are accumulated. Biochemical characterization of this organelle has demonstrated that PM ATPase and the secretory enzyme, acid phosphatase, are transported in a single vesicle species.


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