A 26 S protease subunit that binds ubiquitin conjugates.

  1. Q Deveraux,
  2. V Ustrell,
  3. C Pickart and
  4. M Rechsteiner
  1. Department of Biochemistry, University of Utah School of Medicine, Salt lake City 84132.

    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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