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A more recent version of this article appeared on January 1, 2006
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Submitted on June 10, 2005
Revised on October 12, 2005
Accepted on October 17, 2005
Faculty of Life Sciences, The University of Manchester, Manchester M13 9PT, United Kingdom
Monitoring Editor: Jeffrey Brodsky
We previously showed that thioredoxins are required for DTT tolerance suggesting they maintain redox homeostasis in response to both oxidative and reductive stress conditions. In this present study, we screened the complete set of viable deletion strains in S. cerevisiae for sensitivity to DTT to identify cell functions involved in resistance to reductive stress. 195 mutants were identified, whose gene products are localized throughout the cell. DTT sensitive mutants were distributed among most major biological processes, but particularly affected gene expression, metabolism and the secretory pathway. Strikingly, a mutant lacking TSA1, encoding a peroxiredoxin, showed a similar sensitivity to DTT as a thioredoxin mutant. Epistasis analysis indicated that thioredoxins function upstream of Tsa1 in providing tolerance to DTT. Our data show that the chaperone function of Tsa1, rather than its peroxidase function, is required for this activity. Cells lacking TSA1 were found to accumulate aggregated proteins, and this was exacerbated by exposure to DTT. Analysis of the protein aggregates revealed that they are predominantly composed of ribosomal proteins. Furthermore, aggregation was found to correlate with an inhibition of translation initiation. We propose that Tsa1 normally functions to chaperone misassembled ribosomal proteins, preventing the toxicity that arises from their aggregation.
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