Transcriptional activity is greatly stimulated by promoter-specific activator proteins. These are modular proteins, consisting of a DNA-binding domain and a regulatory (activator) domain. The GAL4 protein of yeast activates the transcription of several genes involved in galactose metabolism. This event requires that GAL4 bind to upstream activation sites with the consensus sequence 5′-CGGN5(T/A)N5CCG-3′ (5 ). A fragment of the GAL4 protein, comprising amino acids 1-147, binds DNA but fails to activate transcription. Linking of an acidic synthetic peptide, forming an α-helix (AH), to this GAL4 DNA-binding domain, results in a protein with an amphipathic structure. This fusion protein is able to activate transcription of a gene, bearing the GAL4 binding sites in an in vitro transcription system by targeting TFIIB in the pre-initiation complex.
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We describe the activities of a wide array of deletion mutants of GAL4, a yeast transcriptional activator. We identify two short regions of GAL4, each of which activates transcription when fused to the DNA-binding region of the molecule. Very large
Proteins that activate genes are quite disparate in character; in particular, some work 'universally' and others do not. A simple model can accommodate most of the recently published results.
Commitment and activation at pol II promoters: a tail of protein-protein interactions.
B Lewin
Cell, 61(7), 1161-1164 (1990-06-29)
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