The proteasome/multicatalytic—multifunctional proteinase In vivo function in the ubiquitin‐dependent N‐end rule pathway of protein degradation in eukaryotes

FEBS Letters

Richter-Ruoff, Birgit¹  Heinemeyer, Wolfgang¹  Wolf, Dieter H.¹ 

[1] Institut für Biochemie der Universität Stuttgart, Pfaffenwaldring 55, D-7000 Stuttgart 80, Germany

关键词: Proteinase yscE;    Proteasome/multicatalytic—multifunctional proteinase;    Ubiquitin;    N-end rule;    Proteolysis;    Yeast;   

DOI  :  10.1016/0014-5793(92)80438-M

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Proteinase yscE, the proteasome/multicatalytic—multifunctional proteinase of yeast had been shown to function in stress response and in the degradation of ubiquitinated proteins [(1991) EMBO J. 10, 555–562]. A well-defined set of proteins degraded via ubiquitin-mediated proteolysis are the substrates of the N-end rule pathway [(1986) Science 234, 179–186; (1989) Science 243, 1576–1583]. We show that mutants defective in the chymotryptic activity of proteinase yscE fail to degrade substrates of the N-end rule pathway. This gives further proof of the proteasome being a central catalyst in ubiquitin-mediated proteolysis.

【 授权许可】

Unknown