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Nucleic Acids Research 2006 34(5):1351-1357; doi:10.1093/nar/gkl012
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Published online 3 March 2006

© The Author 2006. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org


Article

The proteasomal ATPase complex is required for stress-induced transcription in yeast

Rita Sulahian, Stephen Albert Johnston and Thomas Kodadek*

Department of Internal Medicine, Department of Molecular Biology and Department of Microbiology, University of Texas Southwestern Medical Center 5323 Harry Hines Boulevard, Dallas, TX 75390-8573, USA

*To whom correspondence should be addressed at Thomas Kodadek, Julie and Louis Beecherl, Jr Chair in Medical Science, Director, Division of Translational Research, Department of Internal Medicine, UT-Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9185, USA. Tel: +1 214 648 1239; Fax: +1 214 648 4156; Email: Thomas.Kodadek{at}utsouthwestern.edu

Received November 4, 2005. Revised January 25, 2006. Accepted February 13, 2006.

Sug1 and Sug2 are two of six ATPases in the 19S regulatory particle of the 26S proteasome. We have shown previously that these proteins play a non-proteolytic role in the transcription of the GAL genes in yeast. In this study, we probe the requirement for these factors in stress-induced transcription in yeast. It is known that proteasomal proteolysis is not required for these events. Indeed, proteasome inhibitors strongly stimulate expression of these stress response genes. However, shifting strains carrying temperature-sensitive alleles of SUG1 and SUG2 to the restrictive temperature strongly inhibited the expression of HSP26, HSP104 and GAD1 in response to heat shock or treatment with menadione bisulfate. Furthermore, chromatin immunoprecipitation analysis revealed the recruitment of Sug1, Sug2 and Cim5 (another of the ATPases), but not 20S proteasome core proteins, to the promoters of these genes. These data show that the non-proteolytic requirement for the proteasomal ATPases extends beyond the GAL genes in yeast and includes at least the heat and oxidative stress-responsive genes.


Present address: Stephen Albert Johnston Center for Innovations in Medicine, Biodesign institute, Arizona State University, 1001 S. McAllister Avenue, Tempe, AZ 85287-5001, USA


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