Abstract
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 α-helices from two GCN4 monomers, that may be important for interactions with the basic transcriptional machinery.
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Hope, I., Mahadevan, S. & Struhl, K. Structural and functional characterization of the short acidic transcriptional activation region of yeast GCN4 protein. Nature 333, 635–640 (1988). https://doi.org/10.1038/333635a0
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DOI: https://doi.org/10.1038/333635a0
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