Two protein-binding sites in chromatin implicated in the activation of heat-shock genes

Nature. 1984 May 17-23;309(5965):229-34. doi: 10.1038/309229a0.

Abstract

The resistance to exonuclease digestion of two regions of chromatin at the 5' end of heat-shock genes in Drosophila implies they have protein bound to them. The pattern of resistance before and after induction of gene expression suggests that heat-shock genes are activated by the sequential binding of at least two protein factors.

MeSH terms

  • Animals
  • Base Sequence
  • Chromatin / physiology
  • Chromatin / ultrastructure*
  • DNA-Binding Proteins / physiology
  • Deoxyribonucleases
  • Drosophila melanogaster / genetics
  • Exonucleases
  • Gene Expression Regulation*
  • Genes
  • Heat-Shock Proteins / genetics*
  • Operon

Substances

  • Chromatin
  • DNA-Binding Proteins
  • Heat-Shock Proteins
  • Deoxyribonucleases
  • Exonucleases