Inducibility of the HS II Enhancer Depends on Binding of an Erythroid Specific Nuclear Protein

Nucleic Acids Res. 1990 Oct 25;18(20):6011-7. doi: 10.1093/nar/18.20.6011.

Abstract

An erythroid specific, inducible enhancer associated with hypersensitive site II (HS II) plays a central role in the function of the human beta globin dominant control region. The HS II enhancer consists of tandem AP-1 binding sites and has been shown to bind members of the ubiquitous jun and fos families of proteins. The same sites are now shown to bind the erythroid specific protein, NF-E2. Inducibility of the HS II enhancer depends on NF-E2 binding, even in the presence of another hypersensitive site. Further, increased activity of the enhancer in induced K562 cells correlates with the presence of NF-E2, which appears to be present in a modified form. NF-E2 is distinct from some enhancer binding proteins in K562 nuclear extracts, in that it does not contain Fos or Fra-1 protein. Thus, binding by NF-E2 may be the mechanism, whereby tandem AP-1 binding sites confer erythroid specificity on the HS II enhancer.

MeSH terms

  • Base Sequence
  • Cell Line
  • DNA-Binding Proteins / metabolism*
  • Enhancer Elements, Genetic*
  • Erythroid-Specific DNA-Binding Factors
  • Globins / biosynthesis
  • Globins / genetics*
  • Humans
  • Leukemia, Erythroblastic, Acute
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • NF-E2 Transcription Factor
  • NF-E2 Transcription Factor, p45 Subunit
  • Nuclear Proteins / metabolism*
  • Oligonucleotide Probes
  • Plasmids
  • Promoter Regions, Genetic
  • Transcription Factors / metabolism*
  • Transfection

Substances

  • DNA-Binding Proteins
  • Erythroid-Specific DNA-Binding Factors
  • NF-E2 Transcription Factor
  • NF-E2 Transcription Factor, p45 Subunit
  • NFE2 protein, human
  • Nuclear Proteins
  • Oligonucleotide Probes
  • Transcription Factors
  • Globins