Novel Jun- And Fos-related Proteins in Drosophila Are Functionally Homologous to Enhancer Factor AP-1

EMBO J. 1988 Dec 20;7(13):4265-73.

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

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Antigens / genetics
  • Antigens / isolation & purification
  • Binding Sites
  • Biological Evolution
  • DNA / metabolism
  • DNA-Binding Proteins / genetics*
  • DNA-Binding Proteins / immunology
  • DNA-Binding Proteins / isolation & purification
  • Drosophila / genetics*
  • Drosophila / immunology
  • Drosophila / metabolism
  • Humans
  • Molecular Weight
  • Proto-Oncogene Proteins / genetics
  • Proto-Oncogene Proteins / isolation & purification
  • Proto-Oncogene Proteins c-jun
  • Species Specificity
  • Transcription Factors / genetics*
  • Transcription Factors / immunology
  • Transcription Factors / isolation & purification
  • Transcription, Genetic

Substances

  • Antigens
  • DNA-Binding Proteins
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-jun
  • Transcription Factors
  • DNA