The GCR1 gene function is essential for glycogen and trehalose metabolism in Saccharomyces cerevisiae
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
12630316
DOI
10.1007/bf02818668
Knihovny.cz E-zdroje
- MeSH
- DNA vazebné proteiny genetika metabolismus MeSH
- fungální proteiny genetika metabolismus MeSH
- glukoamylasa metabolismus MeSH
- glykogen biosyntéza metabolismus MeSH
- mutace genetika MeSH
- Saccharomyces cerevisiae - proteiny MeSH
- Saccharomyces cerevisiae genetika metabolismus MeSH
- transkripční faktory MeSH
- trehalasa metabolismus MeSH
- trehalosa biosyntéza metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- DNA vazebné proteiny MeSH
- fungální proteiny MeSH
- GCR1 protein, S cerevisiae MeSH Prohlížeč
- glukoamylasa MeSH
- glykogen MeSH
- Saccharomyces cerevisiae - proteiny MeSH
- transkripční faktory MeSH
- trehalasa MeSH
- trehalosa MeSH
Trehalose (Tre) and glycogen (Glg) are synthesized in response to unfavorable growth conditions from glycolytic intermediates in Saccharomyces cerevisiae. Transcription of the glycolytic genes is activated by the Gcr1p complex, the DNA binding transcription factor that directly associates with the CT-box sequences on the promoter region of the glycolytic genes. gcr1 mutant yeast cells cannot utilize glucose effectively. Glg and Tre levels in stationary-phase gcr1 mutant yeast cells were 20-50% of those in the wild-type strain. Likewise, stress-induced accumulation of Tre and Glg in gcr1 mutant cells was significantly lower than in the wild type. In addition, both the synthesis and the degradation of Tre and Glg are very slow in the gcr1 mutant. It seems that Gcr1p function is essential for the coordinated regulation of glycolysis, Tre and Glg metabolism in S. cerevisiae.
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