A 26 S protease subunit that binds ubiquitin conjugates.

Quinn L. Deveraux(University of Utah), Vicença Ustrell(University of Utah), Cecile M. Pickart(University of Utah), Martin Rechsteiner(University of Utah)
Journal of Biological Chemistry
March 1, 1994
10.1016/s0021-9258(17)37244-7
Cited by 764Open Access
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Abstract

Ubiquitin-mediated proteolysis provides an important mechanism for regulating a variety of cellular processes. Ubiquitin-conjugated proteins are degraded by a 26 S protease that contains more than 30 different subunits. Of these, a single 50-kDa polypeptide, subunit 5, specifically binds ubiquitin-lysozyme conjugates. Binding is inhibited by short polymeric chains of ubiquitin but not by ubiquitin monomers or by lysozyme. In addition, subunit 5 binds free ubiquitin chains with efficient association requiring at least four ubiquitins. Thus, proteins conjugated to polymers of ubiquitin may be selected for degradation by a single subunit of the 26 S protease complex.

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