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Vol. 13, Issue 2, 412-424, February 2002
and
Departments of *Biological Sciences, 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, whereas 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 support a model in which Skn7p
receiver domain phosphorylation affects transcriptional activation
rather than DNA binding to this class of DNA binding site.
Biochemistry and
Genetics Ph.D. Program, University of Iowa, University
of Iowa, Iowa City, Iowa 52242; and §National Institute of
Bioscience and Human Technology, Agency of Industrial Science and
Technology, Tsukuba, Ibaraki 305-8566, Japan
Corresponding author. E-mail address:
jan-fassler{at}uiowa.edu.
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