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The proteasome/multicatalytic—multifunctional proteinase In vivo function in the ubiquitin‐dependent N‐end rule pathway of protein degradation in eukaryotes
Author(s) -
Richter-Ruoff Birgit,
Heinemeyer Wolfgang,
Wolf Dieter H.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80438-m
Subject(s) - proteasome , ubiquitin , microbiology and biotechnology , degradation (telecommunications) , protein degradation , in vivo , chemistry , function (biology) , biochemistry , biology , genetics , gene , computer science , telecommunications
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.