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J Biol Chem, Vol. 275, Issue 20, 15182-15192, May 19, 2000

Analysis of a Gene Encoding Rpn10 of the Fission Yeast Proteasome Reveals That the Polyubiquitin-binding Site of This Subunit Is Essential When Rpn12/Mts3 Activity Is Compromised*

Caroline R. M. WilkinsonDagger , Katherine Ferrell§, Mary PenneyDagger , Mairi WallaceDagger , Wolfgang Dubiel§, and Colin GordonDagger

From the Dagger  MRC Human Genetics Unit, Western General Hospital, Crewe Road, Edinburgh, EH4 2XU, Scotland, United Kingdom and § Institute of Biochemistry, Medical Faculty, Humboldt University, Monbijoustrasse 2, 10117 Berlin, Germany

Substrates are targeted for proteolysis by the ubiquitin pathway by the addition of a polyubiquitin chain before being degraded by the 26 S proteasome. Previously, a subunit of the proteasome, S5a, was identified that was able to bind to polyubiquitin in vitro and thus proposed to act as a substrate recognition component. Deletion of the corresponding Saccharomyces cerevisiae gene, MCB1/RPN10, rendered cells viable indicating that other proteasomal polyubiquitin receptors must exist. In this study, we describe pus1+, the fission yeast homologue of RPN10. This gene is also not required for cell viability; however, the Delta pus1 mutant is synthetically lethal with mutations in other proteasomal component-encoding genes, namely mts3, pad1, and mts4 (RPN12, RPN11, and RPN1). Overexpression of pus1+ is able to rescue mts3-1 at 32 °C but overexpression of a cDNA encoding a version of Pus1 that does not bind to polyubiquitin cannot and leads to greatly reduced viability when used to rescue the mts3-1Delta pus1 double mutant. The Mts3 protein was unable to bind to polyubiquitin in vitro, but the Pus1 and Mts3 proteins were found to bind to one another in vitro, which taken together with the genetic data suggests that they are also closely associated in vivo.

* This work was supported by Medical Research Council Funding (to C. W., M. P., M. W., and C. G.) and by a research grant from the Deutsche Forschungsgemeinschaft (to K. F. and W. D.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 131 332 2471; Fax: 131 343 2620; E-mail: colin.gordon@hgu.mrc.ac.uk.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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