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
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Base Sequence
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Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
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Basic-Leucine Zipper Transcription Factors
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DNA / metabolism*
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DNA-Binding Proteins / immunology
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DNA-Binding Proteins / metabolism*
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HeLa Cells / metabolism
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Humans
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Molecular Sequence Data
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Polymers / metabolism
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Precipitin Tests
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Proto-Oncogene Proteins c-myc / immunology
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Proto-Oncogene Proteins c-myc / metabolism*
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Rabbits
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Transcription Factors*
Substances
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Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
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Basic-Leucine Zipper Transcription Factors
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DNA-Binding Proteins
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MAX protein, human
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Myc associated factor X
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Polymers
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Proto-Oncogene Proteins c-myc
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Transcription Factors
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DNA