Saccharomyces cerevisiae Ras/cAMP pathway controls post-diauxic shift element-dependent transcription through the zinc finger protein Gis1.

The Saccharomyces cerevisiae protein kinase Rim15 was identified previously as a component of the Ras/cAMP pathway acting immediately downstream of cAMP-dependent protein kinase (cAPK) to control a broad range of adaptations in response to nutrient limitation. Here, we show that the zinc finger protein Gis1 acts as a dosage-dependent suppressor ...
of the rim15Delta defect in nutrient limitation-induced transcriptional derepression of SSA3. Loss of Gis1 results in a defect in transcriptional derepression upon nutrient limitation of various genes that are negatively regulated by the Ras/cAMP pathway (e.g. SSA3, HSP12 and HSP26). Tests of epistasis as well as transcriptional analyses of Gis1-dependent expression indicate that Gis1 acts in this pathway downstream of Rim15 to mediate transcription from the previously identified post-diauxic shift (PDS) element. Accordingly, deletion of GIS1 partially suppresses, and overexpression of GIS1 exacerbates the growth defect of mutant cells that are compromised for cAPK activity. Moreover, PDS element-driven expression, which is negatively regulated by the Ras/cAMP pathway and which is induced upon nutrient limitation, is almost entirely dependent on the presence of Gis1.
Mesh Terms:
Bacterial Proteins, Binding Sites, Cell Cycle Proteins, Cell Division, Culture Media, Cyclic AMP, Cyclic AMP-Dependent Protein Kinases, DNA, Fungal, Epistasis, Genetic, Fungal Proteins, Gene Dosage, Gene Expression Regulation, Fungal, Genes, Reporter, HSP70 Heat-Shock Proteins, Heat-Shock Proteins, Histone Demethylases, Phosphorylation, Protein Kinases, Protein Processing, Post-Translational, Recombinant Fusion Proteins, Repressor Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Second Messenger Systems, Serine Endopeptidases, Transcription, Genetic, Zinc Fingers, ras Proteins
EMBO J.
Date: Jun. 01, 2000
Download Curated Data For This Publication
16355
Switch View:
  • Interactions 4