Journal article
The Eukaryotic Two-Component Histidine Kinase Sln1p Regulates OCH1 via the Transcription Factor, Skn7p
Molecular biology of the cell, Vol.13(2), pp.412-424
02/2002
DOI: 10.1091/mbc.01-09-0434
PMCID: PMC65637
PMID: 11854400
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.
Details
- Title: Subtitle
- The Eukaryotic Two-Component Histidine Kinase Sln1p Regulates OCH1 via the Transcription Factor, Skn7p
- Creators
- Sheng Li - Departments of Biological Sciences, 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, JapanSusan Dean - Departments of Biological Sciences, 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, JapanZhijian Li - Departments of Biological Sciences, 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, JapanJoe Horecka - Departments of Biological Sciences, 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, JapanRobert J Deschenes - Departments of Biological Sciences, 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, JapanJan S Fassler - Departments of Biological Sciences, 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
- Resource Type
- Journal article
- Publication Details
- Molecular biology of the cell, Vol.13(2), pp.412-424
- DOI
- 10.1091/mbc.01-09-0434
- PMID
- 11854400
- PMCID
- PMC65637
- NLM abbreviation
- Mol Biol Cell
- ISSN
- 1059-1524
- eISSN
- 1939-4586
- Publisher
- The American Society for Cell Biology
- Language
- English
- Date published
- 02/2002
- Academic Unit
- Biology
- Record Identifier
- 9984217534402771
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