Sts1 can overcome the loss of Rad23 and Rpn10 and represents a novel regulator of the ubiquitin/proteasome pathway

Lizbeth Romero-Perez, Li Chen, David Lambertson, Kiran Madura

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

A rad23Δ rpn10Δ 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 rad23Δ rpn10Δ but did not overcome the DNA repair defect of rad23Δ. 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.

Original languageEnglish (US)
Pages (from-to)35574-35582
Number of pages9
JournalJournal of Biological Chemistry
Volume282
Issue number49
DOIs
StatePublished - Dec 7 2007

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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