Essentially - Gal4 was dramatically demonstrated by a...

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Essentially, if the N-terminal domain of the Gal4 protein is deleted, the protein can not bind to the UAS GAL sequence, and so is unable to activate transcription of the reporter gene. But, in addition to DNA binding, Gal4 must have a region near the C-terminal end that is responsible for recruiting and activating the RNA polymerase, thus allowing expression of the reporter gene. The most remarkable thing of all, was that a large region in the center of Gal4 can be deleted; as long as the DNA binding domain is present at the N-terminus, and the activating domain is present at the C-terminus, Gal4 can activate transcription from the UAS GAL sequence. This remarkable separation of function between these two domains of
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Unformatted text preview: Gal4 was dramatically demonstrated by a series of experiments called domain swapping . Essentially, using recombinant DNA techniques, the Gal4 transcription activation domain ( AD ) was fused to the DNA binding ( DB ) domain of an E. coli protein called LexA; LexA is a repressor that binds to a known DNA sequence, the LexA operator ( LexA OP ). Also, the Gal4 DB domain was fused to the AD transcription activation domain of a viral protein know to be a strong activator, VP16. These chimeric proteins were introduced into yeast cells with the appropriate LacZ reporter gene constructs and the results of these domain swapping experiments were dramatic....
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