The proteasome/multicatalytic-multifunctional proteinase. In vivo function in the ubiquitin-dependent N-end rule pathway of protein degradation in eukaryotes.
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.
Richter-Ruoff
B
B
Institut für Biochemie, Universität Stuttgart, Germany.
Heinemeyer
W
W
Wolf
D H
DH
D002384:Catalysis; D002918:Chymotrypsin / Q000378:metabolism; D003546:Cysteine Endopeptidases / Q000235:genetics / Q000378:metabolism*; D009097:Multienzyme Complexes / Q000378:metabolism*; D009154:Mutation; D046988:Proteasome Endopeptidase Complex; D011506:Proteins / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013379:Substrate Specificity; D014452:Ubiquitins / Q000494:pharmacology*; D001616:beta-Galactosidase / Q000378:metabolism
D009097:Multienzyme Complexes; D011506:Proteins; D011993:Recombinant Fusion Proteins; D014452:Ubiquitins; D001616:beta-Galactosidase; D002918:Chymotrypsin; D003546:Cysteine Endopeptidases; C043418:proteinase yscE; D046988:Proteasome Endopeptidase Complex