The HeLa cell protein TEF-1 binds specifically and cooperatively to two SV40 enhancer motifs of unrelated sequence

Cell. 1988 Sep 23;54(7):931-42. doi: 10.1016/0092-8674(88)90108-0.


We have purified a protein (TEF-1) that specifically binds to two sequence unrelated motifs (GT-IIC and Sph) of the simian virus 40 (SV40) enhancer. TEF-1 binds cooperatively to templates containing tandem but not inverted or spaced repeats of its cognate motifs. This cooperative binding correlates with the ability of the tandem repeats to generate enhancer activity in vivo. In contrast, TEF-1 and a second SV40 enhancer binding protein, TEF-2, bind independently to templates containing the cognate motifs of both proteins (GT-I and either GT-IIC or Sph motifs) even though these motifs cooperate in enhancer activity in vivo. These results allow us to distinguish different classes of enhancer factors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allosteric Regulation
  • Binding, Competitive
  • Chromatography, Affinity
  • DNA, Viral / metabolism*
  • DNA-Binding Proteins / isolation & purification
  • DNA-Binding Proteins / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Enhancer Elements, Genetic*
  • HeLa Cells
  • Humans
  • Molecular Weight
  • Mutation
  • Nuclear Proteins*
  • Polyomavirus / genetics
  • Regulatory Sequences, Nucleic Acid
  • Simian virus 40 / genetics*
  • Templates, Genetic
  • Transcription Factors / classification


  • DNA, Viral
  • DNA-Binding Proteins
  • GT-IC protein, human
  • Nuclear Proteins
  • TEAD1 protein, human
  • Transcription Factors