Properties of yeast Saccharomyces cerevisiae plasma membrane dicarboxylate transporter |
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Authors: | D A Aliverdieva D V Mamaev D I Bondarenko K F Sholtz |
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Institution: | (1) Caspian Institute of Biological Resources, Dagestan Research Center, Russian Academy of Sciences, ul. M. Gadgieva 45, 367025 Makhachkala, Russia;(2) Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, 119071 Moscow, Russia |
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Abstract: | Transport of succinate into Saccharomyces cerevisiae cells was determined using the endogenous coupled mitochondrial succinate oxidase system. The dependence of succinate oxidation rate on the substrate concentration was a curve with saturation. At neutral pH the K(m) value of the mitochondrial "succinate oxidase" was fivefold less than that of the cellular "succinate oxidase". O-Palmitoyl-L-malate, not penetrating across the plasma membrane, completely inhibited cell respiration in the presence of succinate but not glucose or pyruvate. The linear inhibition in Dixon plots indicates that the rate of succinate oxidation is limited by its transport across the plasmalemma. O-Palmitoyl-L-malate and L-malate were competitive inhibitors (the K(i) values were 6.6 +/- 1.3 microM and 17.5 +/- 1.1 mM, respectively). The rate of succinate transport was also competitively inhibited by the malonate derivative 2-undecyl malonate (K(i) = 7.8 +/- 1.2 microM) but not phosphate. Succinate transport across the plasma membrane of S. cerevisiae is not coupled with proton transport, but sodium ions are necessary. The plasma membrane of S. cerevisiae is established to have a carrier catalyzing the transport of dicarboxylates (succinate and possibly L-malate and malonate). |
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Keywords: | succinate L-malate malonate O-palmitoyl-L-malate competitive inhibition Saccharomyces cerevisiae plasma membrane dicarboxylate transporter protonophores FCCP and SF sodium symport |
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