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A more recent version of this article appeared on February 1, 2002
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Submitted on August 31, 2001
Revised on October 23, 2001
Accepted on November 7, 2001
1 Department of Biological Sciences and Genetics, University of Iowa, University of Iowa, Iowa City, Iowa 52242
2 Department of Biological Sciences, University of Iowa, University of Iowa, Iowa City, Iowa 52242
3 Department of Biological Sciences, University of Iowa, University of Iowa, Iowa City, Iowa 52242
4 National Institute of Bioscience and Human Technology, Agency of Industrial Science and Technology, Tsukuba, Ibaraki 305-8566, Japan
5 Department of Biochemistry and Genetics, University of Iowa, Iowa City, Iowa 52242
* Corresponding author. E-mail address: jan-fassler{at}uiowa.edu.
The yeast "two-component" osmotic stress phosphorelay consists of the histidine kinase, Sln1p, the phosphorelay intermediate, Ypd1p and two response regulators, Ssk1p and Skn7p whose activities are regulated by phosphorylation of a conserved aspartyl residue in the receiver domain. Dephospho-Ssk1p leads to activation of the hyper-osmotic response (HOG) pathway while phospho-Skn7p presumably leads to activation of hypo-osmotic response genes. The multifunctional Skn7 protein is important in oxidative as well as osmotic stress, however the Skn7p receiver domain aspartate that is the phosphoacceptor in the SLN1 pathway is dispensable for oxidative stress. Like many well-characterized bacterial response regulators, Skn7p is a transcription factor. In this report we investigate the role of Skn7p in osmotic response gene activation. Our studies reveal that the Skn7p HSF-like DNA binding domain interacts with a cis-acting element identified upstream of OCH1 that is distinct from the previously defined HSE-like Skn7p binding site. Our data supports a model in which Skn7p receiver domain phosphorylation affects transcriptional activation rather than DNA binding to this class of DNA binding site.
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