Abstract
Mutagenesis of the fos protein supports the hypothesis that a heptad repeat of leucine residues stabilizes the interaction between the fos and jun proteins. We show that the complex between fos and jun can bind to DNA more tightly than either protein alone and that basic residues adjacent to the leucine repeat of fos contribute to the DNA-binding potential of the complex.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Bacteriophage lambda / metabolism
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Binding Sites
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DNA / metabolism*
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism*
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In Vitro Techniques
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Leucine / physiology*
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Mutation
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Oligonucleotides / metabolism
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Proto-Oncogene Proteins / genetics
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Proto-Oncogene Proteins / metabolism*
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Proto-Oncogene Proteins c-fos
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Proto-Oncogene Proteins c-jun
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Proto-Oncogene Proteins c-myc
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Rabbits
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Transcription Factors / genetics
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Transcription Factors / metabolism*
Substances
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DNA-Binding Proteins
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Oligonucleotides
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Proto-Oncogene Proteins
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Proto-Oncogene Proteins c-fos
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Proto-Oncogene Proteins c-jun
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Proto-Oncogene Proteins c-myc
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Transcription Factors
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DNA
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Leucine