title: Structural and functional characterization of the short acidic transcriptional activation region of yeast GCN4 protein.
abstract: Derivatives of the yeast GCN4 transcription factor containing acidic regions of 35 to 40 amino acids fused directly to the DNA-binding domain are fully functional in vivo. High resolution deletion analysis and proteolytic mapping suggest that the activation region is a repeated structure composed of small units acting additively. Acidic character is a feature of the structural motif, possibly a dimer of alpha-helices from two GCN4 monomers, that may be important for interactions with the basic transcriptional machinery.
authors.affiliation: Department of Biological Chemistry, Harvard Medical School, Boston, Massachusetts 02115.
authors.forename: I A
authors.initials: IA
authors.lastname: Hope
authors.forename: S
authors.initials: S
authors.lastname: Mahadevan
authors.forename: K
authors.initials: K
authors.lastname: Struhl
mesh_terms: D000595:Amino Acid Sequence; D002872:Chromosome Deletion; D004268:DNA-Binding Proteins / Q000235:genetics*; D005656:Fungal Proteins / Q000235:genetics*; D005786:Gene Expression Regulation; D005796:Genes; D005800:Genes, Fungal; D011494:Protein Kinases; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors / Q000235:genetics; D014158:Transcription, Genetic
chemical_list: D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D011494:Protein Kinases