DEGRADATION OF THE YEAST MAT-ALPHA-2 TRANSCRIPTIONAL REGULATOR IS MEDIATED BY THE PROTEASOME

被引：51

作者：

RICHTERRUOFF, B ^{[1
]}

WOLF, DH ^{[1
]}

HOCHSTRASSER, M ^{[1
]}

机构：

[1] UNIV CHICAGO,DEPT BIOCHEM & MOLEC BIOL,CHICAGO,IL 60637

来源：

FEBS LETTERS | 1994年 / 354卷 / 01期

关键词：

PROTEOLYSIS; PROTEASOME; UBIQUITIN; MAT-ALPHA-2; REPRESSOR; SACCHAROMYCES CEREVISIAE;

D O I：

10.1016/0014-5793(94)01085-4

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：

Rapid degradation of specific regulatory proteins plays a role in a wide range of cellular phenomena, including cell cycle progression and the regulation of cell growth and differentiation. A major mechanism of selective protein turnover in vivo involves a large multi-subunit protease known as the proteasome or multi-catalytic proteinase. At the same time, the degradation of many cellular proteins requires their covalent ligation to the polypeptide ubiquitin. Here we show that the yeast S. cerevisiae MAT alpha 2 repressor, which is known to be ubiquitinylated in vivo, requires the proteasome for its rapid intracellular proteolysis.

引用

页码：50 / 52

页数：3

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