Document Detail


The 20S proteasome mediates the degradation of mouse and yeast ornithine decarboxylase in yeast cells.
MedLine Citation:
PMID:  8293806     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Ornithine decarboxylase (ODC), a key enzyme in the biosynthesis of polyamines, is one of the most rapidly degraded proteins in mammalian cells. Recently it has been demonstrated that mammalian ODC is degraded in vitro by the 26S protease that contains the 20S proteasome as its catalytic core, in a reaction that does not require ubiquitin. Here, we show that yeast and mouse ODC are both rapidly degraded in yeast cells and that their degradation severely inhibited in a mutant yeast cell line defective in the chymotryptic activity of proteinase yscE, the yeast 20S proteasome. These results provide compelling genetic support to previous biochemical studies suggesting the involvement of the 20S proteasome in the degradation of ornithine decarboxylase.
Authors:
E Mamroud-Kidron; Y Rosenberg-Hasson; E Rom; C Kahana
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  FEBS letters     Volume:  337     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1994 Jan 
Date Detail:
Created Date:  1994-02-25     Completed Date:  1994-02-25     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  239-42     Citation Subset:  IM    
Affiliation:
Department of Molecular Genetics and Virology, Weizmann Institute of Science, Rehovot, Israel.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cloning, Molecular
Cysteine Endopeptidases / genetics,  metabolism*
Gene Transfer Techniques
Mice
Multienzyme Complexes / metabolism*
Mutation
Ornithine Decarboxylase / genetics,  metabolism*
Proteasome Endopeptidase Complex
Recombinant Proteins / metabolism
Saccharomyces cerevisiae / enzymology*,  genetics
Transformation, Genetic
Chemical
Reg. No./Substance:
0/Multienzyme Complexes; 0/Recombinant Proteins; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.22.-/proteinase yscE; EC 3.4.25.1/Proteasome Endopeptidase Complex; EC 4.1.1.17/Ornithine Decarboxylase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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