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.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Amino Acid Sequence
-
DNA-Binding Proteins / genetics*
-
DNA-Binding Proteins / isolation & purification
-
DNA-Binding Proteins / metabolism
-
Fungal Proteins / genetics*
-
Fungal Proteins / isolation & purification
-
Fungal Proteins / metabolism
-
Metalloproteins / genetics*
-
Metalloproteins / isolation & purification
-
Metalloproteins / metabolism
-
Molecular Sequence Data
-
Mutation*
-
Recombinant Proteins / isolation & purification
-
Saccharomyces cerevisiae / genetics*
-
Transcription Factors / genetics*
-
Transcription Factors / isolation & purification
-
Transcription Factors / metabolism
-
Zinc / metabolism*
Substances
-
DNA-Binding Proteins
-
Fungal Proteins
-
Metalloproteins
-
Recombinant Proteins
-
Transcription Factors
-
Zinc