Altering DNA-binding specificity of GAL4 requires sequences adjacent to the zinc finger

Nature
J C Corton, S A Johnston

Abstract

Many eukaryotic proteins involved in transcriptional regulation contain within their DNA-binding domains a polypeptide loop (the zinc finger) which interacts with DNA. In proteins possessing multiple zinc fingers, including TFIIIA, Sp1, SWI5 and oestrogen/glucocorticoid receptors, the region containing the zinc fingers confers DNA-binding specificity. By contrast, our results demonstrate that all but one of the 28 amino acids encompassing the single zinc-finger region of GAL4, the yeast transcriptional activator, can be replaced with the analogous zinc-finger region from another yeast-activator protein, PPR1, without changing the DNA-binding specificity of GAL4. A 14-amino-acid region adjacent to the zinc finger is necessary for determining specific recognition of DNA sequences.

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Mar 1, 1990·Proceedings of the National Academy of Sciences of the United States of America·T Pan, J E Coleman
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