Abstract
GAL4 is a transcriptional activator found in yeast1,2. Two distinct functions of the protein are required for its activity3–5: one directs sequen1ce-specific DNA binding, and another interacts with some other component of the transcriptional machinery, for example, RNA polymerase II or a TATA-binding protein. Two short regions of GAL4 function as 'activating sequences' when attached to the DNA-binding portion of GAL4 (ref. 6) and these regions can be replaced by a large number of peptides encoded by Escherichia coli genomic DNA fragments7 or by a synthetic peptide designed to form an amphiphilic α-helix8. All of these activating sequences, like that found in another yeast activator, GCN4 (refs 9, 10) bear an excess negative charge (also see ref. 11). GAL4 and its derivatives that are active in yeast stimulate transcription in mammalian cells when GAL4 binding sites are introduced upstream of a mammalian gene12,13; similarly, GAL4 activates transcription in Drosophila cells14. Here we show that GAL4 derivatives stimulate gene expression in plant cells.
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Ma, J., Przibilla, E., Hu, J. et al. Yeast activators stimulate plant gene expression. Nature 334, 631–633 (1988). https://doi.org/10.1038/334631a0
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DOI: https://doi.org/10.1038/334631a0
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