An S1 nuclease-sensitive homopurine/homopyrimidine domain in the PDGF A-chain promoter contains a novel binding site for the growth factor-inducible protein EGR-1

Biochem Biophys Res Commun. 1992 Oct 15;188(1):433-9. doi: 10.1016/0006-291x(92)92403-k.


Transcription of the platelet-derived growth factor (PDGF) A-chain gene is activated in cells exposed to growth factors. We now have identified a homopurine/homopyrimidine domain in the promoter region of the PDGF A-chain gene that exhibits S1 nuclease sensitivity in vitro and that contains a novel binding site (5'-TCCTCCTCCTCCTC-3') for the growth factor inducible transcription factor EGR-1 as demonstrated in gel mobility shift assays. Sequences similar to this novel EGR-1 binding site were observed also in five growth-related genes and shown to bind to EGR-1 in competition assays, suggesting that EGR-1 may influence the transcriptional regulation of these growth-related genes.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Base Sequence
  • Binding Sites
  • DNA-Binding Proteins / biosynthesis
  • DNA-Binding Proteins / metabolism*
  • Growth Substances / pharmacology
  • Macromolecular Substances
  • Molecular Sequence Data
  • Oligodeoxyribonucleotides
  • Platelet-Derived Growth Factor / genetics*
  • Promoter Regions, Genetic*
  • Sequence Homology, Nucleic Acid
  • Single-Strand Specific DNA and RNA Endonucleases / metabolism*
  • Substrate Specificity
  • Transcription Factors / biosynthesis
  • Transcription Factors / metabolism*


  • DNA-Binding Proteins
  • Growth Substances
  • Macromolecular Substances
  • Oligodeoxyribonucleotides
  • Platelet-Derived Growth Factor
  • Transcription Factors
  • Single-Strand Specific DNA and RNA Endonucleases