Degradation of the yeast MATα2 transcriptional regulator is mediated by the proteasome

FEBS Letters

Richter-Ruoff, Birgit²  Wolf, Dieter H.²  Hochstrasser, Mark¹ 

[1] Department of Biochemistry and Molecular Biology, 920 E. 58th Street, University of Chicago, Chicago, IL 60637, USA;Institut für Biochemie der Universität Stuttgart, Pfaffenwaldring 55, 70569 Stuttgart, Germany

关键词: Proteolysis;    Proteasome;    Ubiquitin;    MATα2 repressor;    Saccharomyces cerevisiae;   

DOI  :  10.1016/0014-5793(94)01085-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 MATα2 repressor, which is known to be ubiquitinylated in vivo, requires the proteasome for its rapid intracellular proteolysis.

【 授权许可】

Unknown