The Product of a Fos-Related Gene, Fra-1, Binds Cooperatively to the Ap-1 Site with Jun - Transcription Factor Ap-1 Is Comprised of Multiple Protein Complexes

Cohen, D. R., Ferreira, P. C. P., Gentz, R., Franza, B. R., Curran, T. (February 1989) The Product of a Fos-Related Gene, Fra-1, Binds Cooperatively to the Ap-1 Site with Jun - Transcription Factor Ap-1 Is Comprised of Multiple Protein Complexes. Genes & Development, 3 (2). pp. 173-184. ISSN 0890-9369

Abstract

fra-1 encodes a serum-inducible protein (Fra-1) that is antigenically related to Fos. We have characterized Fra-1 expression in serum-stimulated cells using antibodies raised against several regions of this protein. Fra-1, expressed transiently in COS cells or in serum-stimulated rat fibroblasts, undergoes extensive post-translational modification, primarily by phosphorylation of serine residues. It is present in both the nucleus and the cytoplasm and participates in a protein complex with Jun. Using proteins synthesized in reticulocyte lysates, we have shown that Fra-1, like Fos, binds to the AP-1 recognition element cooperatively with Jun. A truncated Fra-1 protein that contains the leucine zipper region but not an adjacent basic amino acid domain, complexes with Jun in vitro but fails to bind AP-1 oligonucleotides. These results demonstrate that Fra-1 contributes to the DNA-binding activity ascribed to transcription factor AP-1.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > genes: types
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein characterization
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > transcription factor
CSHL Authors:
Communities: CSHL labs
Depositing User: Gail Sherman
Date: February 1989
Date Deposited: 31 Jul 2017 17:52
Last Modified: 31 Jul 2017 17:52
Related URLs:
URI: https://repository.cshl.edu/id/eprint/34838

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