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J. Biol. Chem., Vol. 282, Issue 49, 35574-35582, December 7, 2007

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Sts1 Can Overcome the Loss of Rad23 and Rpn10 and Represents a Novel Regulator of the Ubiquitin/Proteasome Pathway^*

From the Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854

A rad23 rpn10 double mutant accumulates multi-Ub proteins, is deficient in proteolysis, and displays sensitivity to drugs that generate damaged proteins. Overexpression of Sts1 restored normal growth in rad23 rpn10 but did not overcome the DNA repair defect of rad23. To understand the nature of Sts1 suppression, we characterized sts1-2, a temperature-sensitive mutant. We determined that sts1-2 was sensitive to translation inhibitors, accumulated high levels of multi-Ub proteins, and caused stabilization of proteolytic substrates. Additionally, ubiquitinated proteins that were detected in proteasomes were inefficiently cleared in sts1-2. Despite these proteolytic defects, overall proteasome activity was increased in sts1-2. We propose that Sts1 is a new regulatory factor in the ubiquitin/proteasome pathway that controls the turnover of proteasome substrates.

Received for publication, June 13, 2007 , and in revised form, September 10, 2007.

^* This work was supported by National Institutes of Health Grant CA83875. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ These authors contributed equally to this work.

² To whom correspondence should be addressed: Dept. of Biochemistry/RWJMS, 683 Hoes Ln., SPH-Rm. 383, Piscataway, NJ 08854. Tel.: 732-235-5602; Fax: 732-235-4783; E-mail: maduraki{at}umdnj.edu.

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