Publikation: Intracellularly inducible, ubiquitin hydrolase-insensitive tandem ubiquitins inhibit the 26S proteasome activity and cell division
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We constructed polyubiquitin derivatives that contain a tandem repeat of ubiquitins and were insensitive to ubiquitin hydrolases. They were designated tandem ubiquitin (tUb) with the number of repeats, such as tUb2. When tUbs were expressed under the control of the GAL1 promoter in the wild-type yeast strain, growth was strongly inhibited. Under these conditions, the degradation of N-end rule substrates, a UFD substrate and Gcn4 was inhibited, indicating that the tUb inhibits 26S proteasome activity. Consistent with this, tUb binds to the 26S proteasome. We showed that tUb inhibited the in vitro degradation of polyubiquitinylated Sic1 by the 26S proteasome. When tUB6 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.
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SAEKI, Yasushi, Erika ISONO, Tomoko OGUCHI, Masumi SHIMADA, Takayuki SONE, Hiroyuki KAWAHARA, Hideyoshi YOKOSAWA, Akio TOH-E, 2004. Intracellularly inducible, ubiquitin hydrolase-insensitive tandem ubiquitins inhibit the 26S proteasome activity and cell division. In: Genes & Genetic Systems. 2004, 79(2), pp. 77-86. ISSN 1341-7568. eISSN 1880-5779. Available under: doi: 10.1266/ggs.79.77BibTex
@article{Saeki2004Intra-42153, year={2004}, doi={10.1266/ggs.79.77}, title={Intracellularly inducible, ubiquitin hydrolase-insensitive tandem ubiquitins inhibit the 26S proteasome activity and cell division}, number={2}, volume={79}, issn={1341-7568}, journal={Genes & Genetic Systems}, pages={77--86}, author={Saeki, Yasushi and Isono, Erika and Oguchi, Tomoko and Shimada, Masumi and Sone, Takayuki and Kawahara, Hiroyuki and Yokosawa, Hideyoshi and Toh-e, Akio} }
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