Abstract
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.
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Dates
Type | When |
---|---|
Created | 23 years ago (July 25, 2002, 5:09 a.m.) |
Deposited | 1 year, 11 months ago (Sept. 16, 2023, 3:01 a.m.) |
Indexed | 1 year, 9 months ago (Nov. 22, 2023, 10:43 p.m.) |
Issued | 33 years, 3 months ago (May 11, 1992) |
Published | 33 years, 3 months ago (May 11, 1992) |
Published Online | 23 years, 7 months ago (Jan. 16, 2002) |
Published Print | 33 years, 3 months ago (May 11, 1992) |
@article{Richter_Ruoff_1992, title={The proteasome/multicatalytic—multifunctional proteinase In vivo function in the ubiquitin‐dependent N‐end rule pathway of protein degradation in eukaryotes}, volume={302}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/0014-5793(92)80438-m}, DOI={10.1016/0014-5793(92)80438-m}, number={2}, journal={FEBS Letters}, publisher={Wiley}, author={Richter-Ruoff, Birgit and Heinemeyer, Wolfgang and Wolf, Dieter H.}, year={1992}, month=may, pages={192–196} }