Inhibition of ubiquitin/proteasome-dependent proteolysis in Saccharomyces cerevisiae by a Gly-Ala repeat

被引：34

作者：

Heessen, S ^{[1
]}

Dantuma, NP ^{[1
]}

Tessarz, P ^{[1
]}

Jellne, M ^{[1
]}

Masucci, MG ^{[1
]}

机构：

[1] Karolinska Inst, Ctr Microbiol & Tumor Biol, S-17177 Stockholm, Sweden

来源：

FEBS LETTERS | 2003年 / 555卷 / 02期

关键词：

degron; Epstein-Barr virus; green fluorescent protein; N-end rule; proteasome; ubiquitin fusion degradation;

D O I：

10.1016/S0014-5793(03)01296-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The glycine-alanine (GA) repeat of the Epstein-Barr virus nuclear antigen-1 inhibits in cis ubiquitin-dependent proteolysis in mammalian cells through a yet unknown mechanism. In the present study we demonstrate that the GA repeat targets an evolutionarily conserved step in proteolysis since it can prevent the degradation of proteasomal substrates in the yeast Saccharomyces cerevisiae. Insertion of yeast codon-optimised recombinant GA (rGA) repeats of different length in green fluorescent protein reporters harbouring N-end rule or ubiquitin fusion degradation signals resulted in efficient stabilisation of these substrates. Protection was also achieved in rpn10Delta yeast suggesting that this polyubiquitin binding protein is not required for the rGA effect. The conserved effect of the GA repeat in yeast opens the possibility for the use of genetic screens to unravel its mode of action. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：397 / 404

页数：8

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