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	J. Biol. Chem. Dec (2007); 282(49):35574-82
Sts1 can overcome the loss of Rad23 and Rpn10 and represents a novel regulator of the ubiquitin-proteasome pathway-
Romero-Perez L, Chen L, Lambertson D, Madura K
Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA-
Abstract: A rad23Delta rpn10Delta 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 rad23Delta rpn10Delta but did not overcome the DNA repair defect of rad23Delta- 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-
[PUBMED: 17916559]