Structural and functional characterization of the short acidic transcriptional activation region of yeast GCN4 protein

Nature. 1988 Jun 16;333(6174):635-40. doi: 10.1038/333635a0.

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Chromosome Deletion
  • DNA-Binding Proteins / genetics*
  • Fungal Proteins / genetics*
  • Gene Expression Regulation*
  • Genes*
  • Genes, Fungal*
  • Protein Kinases*
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae Proteins*
  • Transcription Factors / genetics
  • Transcription, Genetic*

Substances

  • DNA-Binding Proteins
  • Fungal Proteins
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Protein Kinases