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Novel Jun‐ and Fos‐related proteins in Drosophila are functionally homologous to enhancer factor AP‐1.
Author(s) -
Perkins K. K.,
Dailey G. M.,
Tjian R.
Publication year - 1988
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1988.tb03324.x
Subject(s) - biology , enhancer , transcription factor , dna binding protein , microbiology and biotechnology , dna , transcription (linguistics) , homologous chromosome , nuclear protein , drosophila melanogaster , gene , genetics , linguistics , philosophy
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.