Some characteristics of tetraphenylphosphonium uptake into Saccharomyces cerevisiae

Boxman, A.W.; Barts, P.W.J.A.; Borst-Pauwels, G.W.F.H.

doi:10.1016/0005-2736(82)90146-8

Cited by 40 publications

(10 citation statements)

References 19 publications

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“…This probe of A1R (see Hauer & Hofer, 1978) is taken up by this yeast at a very low rate. As in some other yeasts (Boxman et al, 1982), equilibration takes many hours. Under anaerobic conditions after 6 h of TPP uptake the steady state was not yet achieved.…”

Section: Resultsmentioning

confidence: 92%

The role of ATP in the control of H+-galactoside symport in the yeast Kluyveromyces marxianus

Broek¹,

Bruijne²,

Steveninck³

1987

Biochemical Journal

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Transport of methyl beta-D-thiogalactoside and p-nitrophenyl beta-D-galactoside is shown to proceed through the H+-lactose symporter of Kluyveromyces marxianus. Uptake of these compounds is strongly reduced under anaerobic conditions or aerobically in the presence of antimycin. It is shown that antimycin treatment affects p-nitrophenyl beta-D-galactoside uptake in a similar way as it affects the cellular amount of ATP, suggesting regulation of p-nitrophenyl beta-D-galactoside transport by ATP. Also, manipulation of cellular ATP by antimycin treatment followed by glucose incubation, or by aerobic incubation of cells with 2-deoxy-D-glucose, showed a similar dependence of galactoside uptake on the ATP level. Transport of the lipophilic cation tetraphenylphosphonium is affected by ATP variations in a similar way as galactoside influx. It is concluded that ATP regulates H+-galactoside symport by its influence on charge translocation. It is discussed that a membrane ATPase probably plays a central role in the control of the activity of H+-sugar symport.

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Section: Resultsmentioning

confidence: 92%

The role of ATP in the control of H+-galactoside symport in the yeast Kluyveromyces marxianus

Broek¹,

Bruijne²,

Steveninck³

1987

Biochemical Journal

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“…In the case of S . cerevisiue tetraphenylphosphonium uptake is only partially sensitive to proton ionophores (De la Pena et al, 1982;Boxman et al, 1982;Eraso et al, 1984). Therefore, although there is some correlation between uptake and the energized state of the plasma membrane, its relationship to membrane potential is not so direct as in the other yeast species.…”

Section: Defective Active Transport In Atpase Mutantsmentioning

confidence: 99%

Physiology of mutants with reduced expression of plasma membrane H⁺‐ATPase

Vallejo

Serrano

1989

Yeast

122

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Two mutations containing insertions and deletions in the promoter in the plasma membrane H+-ATPase gene (PMA1) of Saccharomyces cerevisiae have been introduced into the genome by homologous recombination, replacing the wild-type gene. The resulting strains have 15 and 23% of the wild-type ATPase content. Decreased levels of ATPase correlate with decreased rates of proton efflux and decreased uptake rates of amino acids, methylamine, hygromycin B and tetraphenylphosphonium. This supports a central role of the enzyme in yeast bioenergetics. However, the final accumulation gradient of tetraphenylphosphonium is not affected by the mutations and that of methylamine and 2-aminoisobutyric acid is only decreased in the most extreme mutant. Apparently, kinetic constraints seem to prevent the equilibration of yeast active transports with the electrochemical proton gradient. As expected from their transport defects, the ATPase-deficient mutants are more resistant to hygromycin B and more sensitive to acidification than wild-type yeast. Mutant cells are very elongated, suggesting a structural role of the ATPase in the yeast surface.

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“…In Saccharomyces cerevisiae, TPMP + and dimethyldibenzylammonium (DDA + ) (but not TPP + ) are translocated via the inducible thiamin transport system and therefore cannot be used as Δψ probes (Boxman et al, 1982;Barts et al, 1980). However, some natural lipophilic cations do exist, for example, thiamin.…”

Section: Lipophilic Ionsmentioning

confidence: 99%

“…In the presence of 5 μΜ TPB", the initial rate of phosphorylation is inhibited by 20-30%, and Δψ, calculated from the carotenoid shift, is depressed from 210 to 140 mV. Damage due to TPP + has also been ascertained with yeast cells of S. cerevisiae (Boxman et aL, 1982). Damage due to TPP + has also been ascertained with yeast cells of S. cerevisiae (Boxman et aL, 1982).…”

Section: +mentioning

confidence: 99%

Determination of the Proton Electrochemical Gradient across Biological Membranes

Azzone

Pietrobon

Zoratti

1984

Current Topics in Bioenergetics

131

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Some characteristics of tetraphenylphosphonium uptake into Saccharomyces cerevisiae

Cited by 40 publications

References 19 publications

The role of ATP in the control of H+-galactoside symport in the yeast Kluyveromyces marxianus

The role of ATP in the control of H+-galactoside symport in the yeast Kluyveromyces marxianus

Physiology of mutants with reduced expression of plasma membrane H⁺‐ATPase

Determination of the Proton Electrochemical Gradient across Biological Membranes

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Some characteristics of tetraphenylphosphonium uptake into Saccharomyces cerevisiae

Cited by 40 publications

References 19 publications

The role of ATP in the control of H+-galactoside symport in the yeast Kluyveromyces marxianus

The role of ATP in the control of H+-galactoside symport in the yeast Kluyveromyces marxianus

Physiology of mutants with reduced expression of plasma membrane H+‐ATPase

Determination of the Proton Electrochemical Gradient across Biological Membranes

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Product

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Physiology of mutants with reduced expression of plasma membrane H⁺‐ATPase