Expression of the yeast glycogen phosphorylase gene is regulated by stress-response elements and by the HOG MAP kinase pathway
| Autor: | David C. LaPorte, Susan Wohler Sunnarborg, Stephen P. Miller, Indira Unnikrishnan |
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| Rok vydání: | 2001 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Osmotic shock MAP Kinase Signaling System Molecular Sequence Data Bioengineering Saccharomyces cerevisiae Biology medicine.disease_cause Applied Microbiology and Biotechnology Biochemistry Gene Expression Regulation Enzymologic Glycogen phosphorylase chemistry.chemical_compound Osmotic Pressure Gene Expression Regulation Fungal Gene expression Genetics medicine RNA Messenger Cloning Molecular Heat shock Gene Mutation Base Sequence Glycogen Glycogen Phosphorylase Sequence Analysis DNA beta-Galactosidase TATA Box Recombinant Proteins chemistry Mitogen-activated protein kinase Mutagenesis Site-Directed biology.protein Mitogen-Activated Protein Kinases Biotechnology |
| Zdroj: | Yeast. 18:1505-1514 |
| ISSN: | 1097-0061 0749-503X |
| Popis: | Yeast glycogen metabolism responds to environmental stressors such as nutrient limitation and heat shock. This response is mediated, in part, by the regulation of the glycogen metabolic genes. Environmental stressors induce a number of glycogen metabolic genes, including GPH1, which encodes glycogen phosphorylase. Primer extension analysis detected two start sites for GPH1, one of which predominated. Sequences upstream of these sites included a possible TATA element. Mutation of this sequence reduced GPH1 expression by a factor of 10 but did not affect start site selection. This mutation also did not affect the relative induction of GPH1 upon entry into stationary phase. Three candidates for stress response elements (STREs) were found upstream of the TATA sequence. Mutation of the STREs showed that they were required for regulation of GPH1 expression in early stationary phase, and in response to osmotic shock and heat shock. These elements appeared to act synergistically, since the intact promoter exhibited 30-fold more expression in stationary phase than the sum of that observed for each element acting independently. HOG1, which encodes a MAP kinase, has been implicated in control mediated by STREs. For GPH1, induction by osmotic shock depended on a functional HOG1 allele. In contrast, induction upon entry into stationary phase was only partially dependent on HOG1. Furthermore, the heat shock response, which can also be mediated by STREs, was independent of HOG1. These observations suggest that the GPH1 STREs respond to more than one pathway, only one of which requires HOG1. Copyright © 2001 John Wiley & Sons, Ltd. |
| Databáze: | OpenAIRE |
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