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pubmed-article:16338349pubmed:abstractTextAt present, the 26S proteasome-specific inhibitor is not available. We constructed polyubiquitin derivatives that contained a tandem repeat of ubiquitins and were insensitive to ubiquitin hydrolases. When these artificial polyubiquitins (tUbs, tandem ubiquitins) were overproduced in the wild-type yeast strain, growth was strongly inhibited, probably because of inhibition of the 26S proteasome. We also found that several substrates of the ubiquitin-proteasome pathway were stabilized by expressing tUbs in vivo. tUbs containing four units or more of the ubiquitin monomer were found to form a complex with the 26S proteasome. We showed that tUb bound to the 26S proteasome inhibited the in vitro degradation of polyubiquitinylated Sic1 by the 26S proteasome. When tUB6 (six-mer) messenger RNA was injected into Xenopus embryos, cell division was inhibited, suggesting that tUb can be used as a versatile inhibitor of the 26S proteasome.lld:pubmed
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pubmed-article:16338349pubmed:year2005lld:pubmed
pubmed-article:16338349pubmed:articleTitleKnocking out ubiquitin proteasome system function in vivo and in vitro with genetically encodable tandem ubiquitin.lld:pubmed
pubmed-article:16338349pubmed:affiliationDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.lld:pubmed
pubmed-article:16338349pubmed:publicationTypeJournal Articlelld:pubmed
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