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
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
收藏
页码:50 / 52
页数:3
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