Vacuoles: main compartments of potassium, magnesium, and phosphate ions in Saccharomyces carlsbergenis cells

Okorokov, Lev A.; Lichko, L. P.; Kulaev, I. S.

doi:10.1128/jb.144.2.661-665.1980

Cited by 131 publications

(32 citation statements)

References 10 publications

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“…85%) of Li + accumulated in S. cerevisiae X2180-1B was located in the vacuoles. Uptake of Li ÷ resulted in K ÷ efflux from the vacuoles, yeast vacuoles already being identified as the major storage compartment for K + as well as Mg 2÷ and orthophosphate [16,17]. A similar phenomenon has been observed in Na+-grown yeast [18].…”

Section: Discussionmentioning

confidence: 59%

Accumulation and intracellular compartmentation of lithium ions in Saccharomyces cerevisiae

Perkins

1993

FEMS Microbiology Letters

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Accumulation of Li+ in Saccharomyces cerevisiae X2180-1B occurred via an apparent stoichiometric relationship of 1:1 (K+/Li+) when S. cerevisiae was incubated in the presence of 5 and 10 mM LiCl for 3 h. Other cellular cations (Mg2+, Ca2+ and Na+) did not vary on Li+ accumulation, although lithium chemistry dictates a degree of similarity to Group I and II metal cations. Compartmentation of Li+ was mainly in the vacuole which accounted for 85% of the Li+ accumulated after a 6-h incubation period. The remainder was located in the cytosol with negligible amounts being bound to cell fragments including the cell wall. Transmission electron microscopy of Li(+)-loaded cells revealed enlarged vacuoles compared with control cells. This asymmetric cellular distribution may therefore enhance tolerance of S. cerevisiae to Li+ and ensure that essential metabolic processes in the cytosol are not disrupted.

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Section: Discussionmentioning

confidence: 59%

Accumulation and intracellular compartmentation of lithium ions in Saccharomyces cerevisiae

Perkins

1993

FEMS Microbiology Letters

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“…This concentration of free Mg" is very T. V. KULAKOVSKAYA E T A L . close to that in the yeast cytosol, which was found to be 1.35 mM (Okorokov et al, 1980), while the concentration of the osmotically free Mg" is 5mM. Mg2+ was also observed to stimulate arginine transport in the isolated yeast vacuoles; however, this effect was not explained by the authors .…”

Section: Discussionmentioning

confidence: 71%

Transport of organic acid anions and guanosine into vacuoles of Saccharomyces pastorianus

Kulakovskaya

Matys

Okorokov

1991

Yeast

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Isolated vacuoles of the yeast Saccharomyces pastorianus accumulate citrate, α‐ketoglutarate, malate and guanosine. This accumulation is Mg ATP‐dependent and inhibited by protonophores. The ionophores monensin and A23187 (electroneutral Men+/nH+‐exchange) inhibit guanosine accumulation but fail to block citrate uptake. Mg2+ ions (2 mM) increase the values of both Δ\documentclass{article}\pagestyle{empty}\begin{document}$ \tilde \mu $\end{document}H+ components and stimulate the uptake of all the above compounds. Ca2+ ions (1 mM), hyperpolarizing the yeast vacuolar membrane and dissipating the pH gradient, inhibit guanosine uptake and stimulate that of citrate. It is concluded that guanosine is transported into yeast vacuoles by an H+/guanosine antiporter while citrate, malate and α‐ketoglutarate are translocated by a uniporter(s) at the expense of the membrane potential (positive inside).

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“…This led us to assume that some vacuolar salt component might be the additional factor enabling proteinase yscA to mature pro-carboxypeptidase yscY. A characteristic vacuolar component is polyphosphate (Urech et al, 1978;Okorokov et al, 1980). Addition of a polyphosphoric acid mixture or sodium polyphosphate of defined chain length to purified proteinase yscA led to activation (Table I) and maturation (not shown) of pro-carboxypeptidase yscY.…”

Section: Resultsmentioning

confidence: 99%

Maturation of vacuolar (lysosomal) enzymes in yeast: proteinase yscA and proteinase yscB are catalysts of the processing and activation event of carboxypeptidase yscY.

1987

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Studies were performed to unravel the activation and maturation mechanism of vacuolar (lysosomal) proteinases in Saccharomyces cerevisiae. In vivo and in vitro studies show that proteinase yscA and proteinase yscB are involved in the activation and processing event of pro‐carboxypeptidase yscY. Processing and activation of pro‐carboxypeptidase yscY by proteinase yscA depends on an additional factor contained in the vacuolar fraction. Comparable activation can be mimicked by sodium polyphosphate. Optimum pH for processing by this proteinase yscA‐triggered event is 5. The proteinase yscA‐triggered maturation process of pro‐carboxypeptidase yscY leads to an intermediate mol. wt form of the enzyme which is, however, fully active. Proteinase yscB transfers the intermediate mol. wt form of the original precursor to the apparently authentic, mature and active carboxypeptidase yscY. An activation and maturation scheme is devised.

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Vacuoles: main compartments of potassium, magnesium, and phosphate ions in Saccharomyces carlsbergenis cells

Cited by 131 publications

References 10 publications

Accumulation and intracellular compartmentation of lithium ions in Saccharomyces cerevisiae

Accumulation and intracellular compartmentation of lithium ions in Saccharomyces cerevisiae

Transport of organic acid anions and guanosine into vacuoles of Saccharomyces pastorianus

Maturation of vacuolar (lysosomal) enzymes in yeast: proteinase yscA and proteinase yscB are catalysts of the processing and activation event of carboxypeptidase yscY.

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