Direct measurements of the initial velocity of entrance of C(14)-labelled L-arginine into yeast cells show that most of the amino acids do not inhibit L-arginine uptake under our experimental conditions. Only the basic amino acids L-canavanine, L-lysine, L-ornithine, L-histidine and D-arginine were inhibitory. L-Citrulline and structurally related derivatives of arginine or basic amino acids (agmatine, cadaverine, putrescine, glyeocyamine, creatine) had no effect. Among the inhibitory amino acids, L-canavanine, L-lysine, L-ornithine and D-arginine exert a competitive inhibition, while L-histidine exerted an inhibition of mixed type. Mutants resistant to L-canavanine were isolated in which the uptake of L-arginine is specifically impaired. Genetic analysis shows that the mutation is recessive, that it presents a gene-dose effect and segregates normally as a single gene. The physiological behaviour of the mutants under a variety of conditions is in agreement with the above observations. It is concluded that a specific transport system exists for L-arginine in yeast.

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Journal Article

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Grenson M, Mousset M, Wiame JM, Bechet J

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