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• W1991167254 endingPage "144" @default.
• W1991167254 startingPage "139" @default.
• W1991167254 abstract "Ornithine decarboxylase (ODC), the first rate-limiting enzyme in the polyamine biosynthesis is one of the most rapidly degraded proteins in eukaryotic cells. Mammalian ODC is a notable exception to the widely accepted dogma that ubiquitination is always required for targeting a protein to degradation by the 26S proteasome. However, while it is well established that in mammalian cells degradation of ODC is ubiquitin independent, the requirement of ubiquitination for degradation of ODC in yeast cells remained undetermined. We have investigated ODC degradation in three mutant strains of Saccharomyces cerevisiae in which ubiquitin-dependent protein degradation activity is severely compromised. While yeast ODC was rapidly degraded in all these mutant strains the degradation of N-end rule substrates was inhibited. A mutant mouse ODC that fails to interact with Az was rapidly degraded in yeast cells but was stable in mammalian cells suggesting that interaction with a mammalian Az like yeast protein is not necessary for the degradation of ODC in yeast cells. Deletion analysis revealed that sequences from its unique N-terminus are involved in targeting yeast ODC to rapid degradation in yeast cells." @default.
• W1991167254 created "2016-06-24" @default.
• W1991167254 creator A5022226268 @default.
• W1991167254 creator A5064008475 @default.
• W1991167254 date "2002-04-01" @default.
• W1991167254 modified "2023-10-14" @default.
• W1991167254 title "Degradation of ornithine decarboxylase in Saccharomyces cerevisiae is ubiquitin independent" @default.
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• W1991167254 doi "https://doi.org/10.1016/s0006-291x(02)00194-8" @default.
• W1991167254 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12054575" @default.
• W1991167254 hasPublicationYear "2002" @default.
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