Sequence-specific DNA binding by the c-Myc protein

Science. 1990 Nov 23;250(4984):1149-51. doi: 10.1126/science.2251503.


While it has been known for some time that the c-Myc protein binds to random DNA sequences, no sequence-specific binding activity has been detected. At its carboxyl terminus, c-Myc contains a basic--helix-loop-helix (bHLH) motif, which is important for dimerization and specific DNA binding, as demonstrated for other bHLH protein family members. Of those studied, most bHLH proteins bind to sites that contain a CA- -TG consensus. In this study, the technique of selected and amplified binding-sequence (SAAB) imprinting was used to identify a DNA sequence that was recognized by c-Myc. A purified carboxyl-terminal fragment of human c-Myc that contained the bHLH domain bound in vitro in a sequence-specific manner to the sequence, CACGTG. These results suggest that some of the biological functions of Myc family proteins are accomplished by sequence-specific DNA binding that is mediated by the carboxyl-terminal region of the protein.

Publication types

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

MeSH terms

  • Base Sequence
  • Binding Sites
  • DNA / metabolism*
  • Glutathione Transferase
  • Leucine Zippers
  • Macromolecular Substances
  • Molecular Sequence Data
  • Oligonucleotides / metabolism
  • Polymerase Chain Reaction
  • Protein Conformation
  • Proto-Oncogene Proteins c-myc / metabolism*
  • Recombinant Fusion Proteins / metabolism
  • Templates, Genetic


  • Macromolecular Substances
  • Oligonucleotides
  • Proto-Oncogene Proteins c-myc
  • Recombinant Fusion Proteins
  • DNA
  • Glutathione Transferase