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MBC in Press, published online ahead of print March 14, 2007
Mol. Biol. Cell 10.1091/mbc.E06-10-0965

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Submitted on October 30, 2006
Revised on February 20, 2007
Accepted on March 1, 2007

A Conditional Yeast E1 Mutant Blocks the Ubiquitin-Proteasome Pathway and Reveals a Role for Ubiquitin Conjugates in Targeting Rad23 to the Proteasome

Nazli Ghaboosi and Raymond J. Deshaies

Howard Hughes Medical Institute, Division of Biology, California Institute of Technology, Pasadena, CA 91125

Monitoring Editor: William Tansey

E1 ubiquitin activating enzyme catalyzes the initial step in all ubiquitin-dependent processes. We report the isolation of uba1-204, a temperature-sensitive allele of the essential S. cerevisiae E1 gene, UBA1. Uba1-204 cells exhibit dramatic inhibition of the ubiquitin-proteasome system, resulting in rapid depletion of cellular ubiquitin conjugates and stabilization of multiple substrates. We have used the tight phenotype of this mutant to investigate the role ubiquitin conjugates play in the dynamic interaction of the UbL/UBA domain adaptor proteins Rad23 and Dsk2 with the proteasome. Although proteasomes purified from mutant cells are intact and proteolytically active, they are depleted of ubiquitin conjugates, Rad23, and Dsk2. Binding of Rad23 to these proteasomes in vitro is enhanced by addition of either free or substrate-linked ubiquitin chains. Moreover, association of Rad23 with proteasomes in mutant and wild-type cells is improved upon stabilizing ubiquitin conjugates with proteasome inhibitor. We propose that recognition of polyubiquitin chains by Rad23 promotes its shuttling to the proteasome in vivo.

Address correspondence to: Raymond J. Deshaies (deshaies{at}caltech.edu)




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