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Originally published in Science Express on 15 August 2002
Science 18 October 2002:
Vol. 298. no. 5593, pp. 611 - 615
DOI: 10.1126/science.1075898
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Reports

Role of Rpn11 Metalloprotease in Deubiquitination and Degradation by the 26S Proteasome

Rati Verma,1 L. Aravind,2 Robert Oania,1 W. Hayes McDonald,3 John R. Yates III,3 Eugene V. Koonin,2 Raymond J. Deshaies1*

The 26S proteasome mediates degradation of ubiquitin-conjugated proteins. Although ubiquitin is recycled from proteasome substrates, the molecular basis of deubiquitination at the proteasome and its relation to substrate degradation remain unknown. The Rpn11 subunit of the proteasome lid subcomplex contains a highly conserved Jab1/MPN domain-associated metalloisopeptidase (JAMM) motif--EXnHXHX10D. Mutation of the predicted active-site histidines to alanine (rpn11AXA) was lethal and stabilized ubiquitin pathway substrates in yeast. Rpn11AXA mutant proteasomes assembled normally but failed to either deubiquitinate or degrade ubiquitinated Sic1 in vitro. Our findings reveal an unexpected coupling between substrate deubiquitination and degradation and suggest a unifying rationale for the presence of the lid in eukaryotic proteasomes.

1 Department of Biology and Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.
2 National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.
3 Department of Cell Biology, The Scripps Research Institute, San Diego, CA 92037, USA.
*   To whom correspondence should be addressed. E-mail: deshaies{at}caltech.edu

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