TY - JOUR

T1 - Post-translational fate of CAN1 permease of Saccharomyces cerevisiae

AU - Opekarová, M

AU - Caspari, T

AU - Pinson, B

AU - Bréthes, D

AU - Tanner, W

PY - 1998/2

Y1 - 1998/2

N2 - 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.

AB - 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.

KW - Blotting, Western

KW - Electrophoresis, Polyacrylamide Gel

KW - Fungal Proteins

KW - Luminescent Measurements

KW - Membrane Transport Proteins

KW - Nitrogen

KW - Phosphorylation

KW - Plasmids

KW - Protein Processing, Post-Translational

KW - Saccharomyces cerevisiae

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1002/(SICI)1097-0061(199802)14:3<215::AID-YEA214>3.0.CO;2-3

DO - 10.1002/(SICI)1097-0061(199802)14:3<215::AID-YEA214>3.0.CO;2-3

M3 - Article

C2 - 9544242

VL - 14

SP - 215

EP - 224

JO - Yeast

JF - Yeast

SN - 0749-503X

IS - 3

ER -