Max and c-Myc/Max DNA-binding activities in cell extracts

Oncogene. 1992 Sep;7(9):1783-92.

Abstract

We have examined the interactions and DNA-binding activities of the c-Myc oncoprotein and its partner Max. In cell extracts virtually all c-Myc molecules are associated with Max in heterodimeric complexes. Moreover, DNA-binding studies with in vitro-translated protein and cell extracts show that both Max alone and c-Myc/Max bind the same DNA sequence. Conversely, c-Myc is unable to bind this sequence in the absence of Max. These findings suggest that c-Myc may function via obligate complex formation with Max.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
  • Basic-Leucine Zipper Transcription Factors
  • DNA / metabolism*
  • DNA-Binding Proteins / immunology
  • DNA-Binding Proteins / metabolism*
  • HeLa Cells / metabolism
  • Humans
  • Molecular Sequence Data
  • Polymers / metabolism
  • Precipitin Tests
  • Proto-Oncogene Proteins c-myc / immunology
  • Proto-Oncogene Proteins c-myc / metabolism*
  • Rabbits
  • Transcription Factors*

Substances

  • Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
  • Basic-Leucine Zipper Transcription Factors
  • DNA-Binding Proteins
  • MAX protein, human
  • Myc associated factor X
  • Polymers
  • Proto-Oncogene Proteins c-myc
  • Transcription Factors
  • DNA