Abstract
A homolog of mammalian enhancer binding factor AP-1 was detected in Drosophila and was purified from embryo nuclear extracts by sequence-specific DNA affinity chromatography. The purified fraction, dAP-1, displays the sequence specificity as well as transcriptional activation properties of mammalian AP-1 and consists of two major proteins of mol. wts 40 and 70 kd. Antibody cross-reactivity experiments suggest that these proteins are Drosophila homologs of proto-oncogene products, Jun and Fos. The Drosophila Jun- and Fos-related antigens, when separated, are individually capable of sequence-specific DNA binding, and the Jun-related antigen activates transcription in vitro.
Publication types
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Comparative Study
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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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Antigens / genetics
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Antigens / isolation & purification
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Binding Sites
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Biological Evolution
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DNA / metabolism
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DNA-Binding Proteins / genetics*
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DNA-Binding Proteins / immunology
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DNA-Binding Proteins / isolation & purification
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Drosophila / genetics*
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Drosophila / immunology
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Drosophila / metabolism
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Humans
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Molecular Weight
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Proto-Oncogene Mas
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Proto-Oncogene Proteins / genetics
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Proto-Oncogene Proteins / isolation & purification
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Proto-Oncogene Proteins c-jun
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Species Specificity
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Transcription Factors / genetics*
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Transcription Factors / immunology
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Transcription Factors / isolation & purification
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Transcription, Genetic
Substances
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Antigens
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DNA-Binding Proteins
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MAS1 protein, human
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Proto-Oncogene Mas
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Proto-Oncogene Proteins
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Proto-Oncogene Proteins c-jun
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Transcription Factors
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DNA