Max and c-Myc/Max DNA-binding activities in cell extracts.
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.
Littlewood
T D
TD
Biochemistry of the Cell Nucleus Laboratory, Imperial Cancer Research Fund, London, UK.
Amati
B
B
Land
H
H
Evan
G I
GI
D000818:Animals; D001483:Base Sequence; D051778:Basic Helix-Loop-Helix Leucine Zipper Transcription Factors; D050976:Basic-Leucine Zipper Transcription Factors; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000276:immunology / Q000378:metabolism*; D006367:HeLa Cells / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D011108:Polymers / Q000378:metabolism; D011233:Precipitin Tests; D016271:Proto-Oncogene Proteins c-myc / Q000276:immunology / Q000378:metabolism*; D011817:Rabbits; D014157:Transcription Factors
D051778:Basic Helix-Loop-Helix Leucine Zipper Transcription Factors; D050976:Basic-Leucine Zipper Transcription Factors; D004268:DNA-Binding Proteins; C499330:MAX protein, human; C067850:Myc associated factor X; D011108:Polymers; D016271:Proto-Oncogene Proteins c-myc; D014157:Transcription Factors; D004247:DNA