Open AccessGCR1 of Saccharomyces cerevisiae encodes a DNA binding protein whose binding is abolished by mutations in the CTTCC sequence motif.
Author(s) -
Henry V. Baker
Publication year - 1991
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.88.21.9443
Subject(s) - gene , activator (genetics) , mutant , biology , saccharomyces cerevisiae , dna , gene product , sequence motif , binding site , dna binding protein , repressor , gene expression , dna binding site , biochemistry , genetics , transcription factor , promoter
In Saccharomyces cerevisiae, glycolysis enzymes constitute 30-60% of the soluble protein. GCR1 gene function is required for high-level glycolytic gene expression. In gcr1 mutant strains the levels of most glycolytic enzymes are between 2% and 10% of wild type. Binding sites for the global regulatory protein known as repressor activator protein 1 (RAP1)/general regulatory factor 1 (GRF1)/translation upstream factor (TUF) are found in close proximity to one or more CTTCC sequence motifs in the controlling region of GCR1-dependent genes. RAP1/GRF1/TUF-binding sites are known to be essential elements of upstream activating sequences that control expression of many glycolytic genes. In this report, I demonstrate that GCR1 encodes a DNA binding protein whose ability to bind DNA is dependent on the CTTCC sequence motif. This finding, in addition to the work of others, suggests that the GCR1 gene product and the RAP1/GRF1/TUF gene product act in concert to mediate high-level glycolytic gene expression.