ArticleGenetics1995
Mutations in GCR1, a transcriptional activator of Saccharomyces cerevisiae glycolytic genes, function as suppressors of gcr2 mutations.
Article in Genetics, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 27 citations in OpenAlex.
- Adaptive Response ofJournal of fungi (Basel, Switzerland) · 2022Article
- Widespread use of non-productive alternative splice sites in Saccharomyces cerevisiae.PLoS genetics · 2014Article
- Osmotic stress signaling and osmoadaptation in yeasts.Microbiology and molecular biology reviews : MMBR · 2002Review
- Rap1p requires Gcr1p and Gcr2p homodimers to activate ribosomal protein and glycolytic genes, respectively.Genetics · 2001Article
- A novel TATA-binding protein-binding protein, ABT1, activates basal transcription and has a yeast homolog that is essential for growth.Molecular and cellular biology · 2000Article
- Glucose metabolism in gcr mutants of Saccharomyces cerevisiae.Journal of bacteriology · 1999Article
- The role of Gcr1p in the transcriptional activation of glycolytic genes in yeast Saccharomyces cerevisiae.Genetics · 1997Article
- Article
- Activation mechanism of the multifunctional transcription factor repressor-activator protein 1 (Rap1p).Molecular and cellular biology · 1996Article
- Article
- Control of glycolytic gene expression in the budding yeast (Saccharomyces cerevisiae).Current genetics · 1995Review
- Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Saccharomyces cerevisiae GCR1 and GCR2 genes affect expression of most of the glycolytic genes. Evidence for Gcr1p/Gcr2p interaction has been presented earlier and is now supported by the isolation of mutations in Gcr1p suppressing gcr2, as assessed by growth and enzyme assay. Four specific mutation sites were identified. Together with use of the two-hybrid system of Fields and Song, they show that Gcr1p in its N-terminal half has a potential transcriptional activating function as well as elements for interaction with Gcr2p, which perhaps acts normally to expose an otherwise cryptic activation domain on Gcr1p. Complementation of various gcr1 mutant alleles and results with the two-hybrid system also indicate that Gcr1p itself normally functions as an oligomer.
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Registered trials
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