Structural and functional characterization of the short acidic transcriptional activation region of yeast GCN4 protein

• DOI: 10.1038/333635a0
• Publication Date: 2003-06-12T21:57:37Z
• Authors: Ian A. Hope; Subramony Mahadevan; Kevin Struhl
• Keywords: 0303 health sciences; Saccharomyces cerevisiae Proteins; Transcription, Genetic; Genes, Fungal; Saccharomyces cerevisiae; DNA-Binding Proteins; Fungal Proteins; 03 medical and health sciences; Gene Expression Regulation; Genes; Amino Acid Sequence; Chromosome Deletion; Protein Kinases; Transcription Factors

Derivatives of the yeast GCN4 transcription factor containing acidic regions of 35 to 40 amino acids fused directly to the DNA-binding domain are fully functional in vivo. High resolution deletion analysis and proteolytic mapping suggest that the activation region is a repeated structure composed of small units acting additively. Acidic character is a feature of the structural motif, possibly a dimer of alpha-helices from two GCN4 monomers, that may be important for interactions with the basic transcriptional machinery.