A CACGTG motif of the Antirrhinum majus chalcone synthase promoter is recognized by an evolutionarily conserved nuclear protein

Proc Natl Acad Sci U S A. 1989 Sep;86(18):6930-4. doi: 10.1073/pnas.86.18.6930.

Abstract

In the chalcone synthase gene of Antirrhinum majus (snapdragon), 150 base pairs of the 5' flanking region contain cis-acting signals for UV light-induced expression. A nuclear factor, designated CG-1, specifically recognizes a hexameric motif with internal dyad symmetry, CACGTG, located within this light-responsive sequence. Binding of CG-1 is influenced by C-methylation of the CpG dinucleotide in the recognition sequence. CG-1 is a factor found in a variety of dicotyledonous plant species including Nicotiana tabacum, A. majus, Petunia hybrida, Arabidopsis thaliana, and Glycine max. CACGTG motifs contained within trans-acting factor recognition sites in various other plant promoters can interact with CG-1. In addition, the binding site of the human adenovirus major late transcription factor USF can compete for CG-1 binding to the chalcone synthase promoter. This suggests an evolutionary conservation of trans-acting factor recognition sites involved in divergent mechanisms of gene control.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyltransferases / genetics*
  • Base Sequence
  • Biological Evolution*
  • Genes*
  • Molecular Sequence Data
  • Nicotiana / metabolism
  • Nuclear Proteins / genetics*
  • Nuclear Proteins / metabolism
  • Oligonucleotide Probes
  • Plants / enzymology
  • Plants / genetics*
  • Plants, Toxic
  • Promoter Regions, Genetic*
  • Protein Binding

Substances

  • Nuclear Proteins
  • Oligonucleotide Probes
  • Acyltransferases
  • flavanone synthetase