Catabolite inactivation of the yeast maltose transporter requires ubiquitin-ligase npi1/rsp5 and ubiquitin-hydrolase npi2/doa4

被引：56

作者：

Lucero, P ^{[1
]}

Lagunas, R ^{[1
]}

机构：

[1] CSIC, INST INVEST BIOMED, E-28029 MADRID, SPAIN

来源：

FEMS MICROBIOLOGY LETTERS | 1997年 / 147卷 / 02期

关键词：

catabolite inactivation; endocytosis; maltose transporter; proteolysis; ubiquitin pathway; Saccharomyces cerevisiae;

D O I：

10.1016/S0378-1097(96)00538-1

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The maltose transporter in Saccharomyces cerevisiae is degraded in the vacuole after internalization by endocytosis when protein synthesis is impaired and a fermentable substrate is present. The possible implication of the ubiquitin pathway in this inactivation, known as catabolite inactivation, has been investigated. Using mutants deficient in npi1/rsp5 ubiquitin-protein ligase and npi2/doa4 ubiquitin-protein hydrolase, we have shown that these two enzymes are required for normal endocytosis and degradation of the transporter. These facts indicate that the ubiquitin pathway is involved in catabolite inactivation of the maltose transporter. The results also revealed that both enzymes act in the internalization step of endocytosis.

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页码：273 / 277

页数：5

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