The eukaryotic two-component histidine kinase Sln1p regulates OCH1 via the transcription factor, Skn7p.

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.
Mesh Terms:
Aspartic Acid, Binding Sites, Cell Wall, DNA-Binding Proteins, Fungal Proteins, Gene Expression Regulation, Fungal, Intracellular Signaling Peptides and Proteins, Mannosyltransferases, Membrane Glycoproteins, Promoter Regions, Genetic, Protein Kinases, Response Elements, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Analysis, DNA, Signal Transduction, Terminal Repeat Sequences, Transcription Factors, Transcriptional Activation
Mol. Biol. Cell
Date: Feb. 01, 2002
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