1. Altering DNA-binding specificity of GAL4 requires sequences adjacent to the zinc finger
- Author
-
Corton Jc and Stephen Albert Johnston
- Subjects
chemistry.chemical_classification ,Zinc finger ,Multidisciplinary ,biology ,Saccharomyces cerevisiae ,Molecular Sequence Data ,biology.organism_classification ,DNA-binding protein ,Yeast ,DNA sequencing ,Recombinant Proteins ,Amino acid ,DNA-Binding Proteins ,Fungal Proteins ,Zinc ,Biochemistry ,chemistry ,Transcription (biology) ,Metalloproteins ,Mutation ,Transcriptional regulation ,Amino Acid Sequence ,Transcription Factors - Abstract
MANY eukaryotic proteins involved in transcriptional regulation contain within their DNA-binding domains a polypeptide loop (the zinc finger) which interacts with DNA1,2. In proteins possessing multiple zinc fingers, including TFIIIA3, Spl4,5, SWI56 and oestrogen/glucocorticoid receptors7, 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.
- Published
- 1989