title: Structural motif of the GCN4 DNA binding domain characterized by affinity cleaving.
abstract: The NH2-terminal locations of a dimer containing the DNA binding domain of the yeast transcriptional activator GCN4 have been mapped on the binding sites 5'-CTGACTAAT-3' and 5'-ATGACTCTT-3'. Affinity cleaving was effected by synthetic GCN4 proteins with Fe.EDTA moieties at the NH2-terminus. Analysis of the DNA cleavage patterns for dimers of the Fe.EDTA-proteins corresponding to GCN4 residues 222 to 281 and 226 to 281 revealed that the NH2-termini were in the major groove nine to ten base pairs apart and were symmetrically displaced four to five base pairs from the central C of the recognition site. This result is consistent with the Y-shaped scissor grip-leucine zipper model recently proposed for a class of DNA binding proteins important in the regulation of gene expression.
authors.affiliation: Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.
authors.forename: M G
authors.initials: MG
authors.lastname: Oakley
authors.forename: P B
authors.initials: PB
authors.lastname: Dervan
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins; D004492:Edetic Acid / Q000378:metabolism; D005290:Ferric Compounds / Q000378:metabolism; D005656:Fungal Proteins / Q000378:metabolism*; D007930:Leucine; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011494:Protein Kinases; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors / Q000378:metabolism*
chemical_list: D004268:DNA-Binding Proteins; D005290:Ferric Compounds; D005656:Fungal Proteins; D046911:Macromolecular Substances; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D004247:DNA; D004492:Edetic Acid; D011494:Protein Kinases; D007930:Leucine; C019179:Fe(III)-EDTA