Post-translational fate of CAN1 permease of Saccharomyces cerevisiae

Opekarova, Miroslava and Caspari, Thomas and Pinson, Benoit and Bréthes, Daniel and Tanner, Widmar (1998) Post-translational fate of CAN1 permease of Saccharomyces cerevisiae. YEAST, 14 (3). pp. 215-224. ISSN 0749-503X, 1097-0061

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Abstract

To study the post-translational fate of arginine permease (Can1p), the gene coding for this transport protein was placed behind a constitutive promoter of plasma membrane ATPase (PMA1) and furnished with a Myc tag. In exponential-phase cells the amount of Can1p is constant, although turnover can be demonstrated. A rapid decrease in transport activity during the early stationary phase is paralleled by a corresponding net degradation of the protein. The amount of Can1p present in exponential cells grown on various nitrogen sources is the same, except in arginine-grown cells, in which the amount of the protein is markedly lower. This occurs solely when arginine serves as nitrogen source but not as an immediate consequence of for example, arginine addition to cells growing on other nitrogen sources. It was demonstrated that Can1p is phosphorylated. Since Can1p expression under the PMA1 promoter is glucose-dependent, the amount of the permease expressed in high-glucose-grown cells is higher than in low-glucose-grown ones. Only a part of the Can1p overexpressed in high-glucose-grown cells is phosphorylated, while in low-glucose-grown cells the phosphorylated form probably represents the majority of Can1p. The permease phosphorylation or dephosphorylation is not related to transinhibition. (C) 1998 John Wiley & Sons, Ltd.

Item Type: Article
Uncontrolled Keywords: PLASMA-MEMBRANE ATPASE; YEAST URACIL PERMEASE; AMINO-ACID PERMEASES; PROTEIN-KINASE; GENE DOSAGE; DEGRADATION; ENDOCYTOSIS; VACUOLE; PHOSPHORYLATION; IDENTIFICATION; Saccharomyces cerevisiae; arginine permease; turnover; phosphorylation
Subjects: 500 Science > 580 Botanical sciences
Divisions: Biology, Preclinical Medicine > Institut für Pflanzenwissenschaften > Lehrstuhl für Zellbiologie und Pflanzenphysiologie (Prof. Dr. Klaus Grasser)
Depositing User: Dr. Gernot Deinzer
Date Deposited: 24 Oct 2023 08:07
Last Modified: 24 Oct 2023 08:07
URI: https://pred.uni-regensburg.de/id/eprint/50144

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