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

Abstract:

: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.

journal_name

Mol Biol Cell

authors

Li S,Dean S,Li Z,Horecka J,Deschenes RJ,Fassler JS

doi

10.1091/mbc.01-09-0434

keywords:

subject

Has Abstract

pub_date

2002-02-01 00:00:00

pages

412-24

issue

2

eissn

1059-1524

issn

1939-4586

journal_volume

13

pub_type

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