Isolation and characterization of a fourth Arabidopsis thaliana G-box-binding factor, which has similarities to Fos oncoprotein.
A fourth member of the Arabidopsis G-box-binding factor (GBF) family of bZIP proteins, GBF4, has been isolated and characterized. In a manner reminiscent of the Fos-related oncoproteins of mammalian systems, GBF4 cannot bind to DNA as a homodimer, although it contains a basic region capable of specifically recognizing the G-box ... and G-box-like elements. However, GBF4 can interact with GBF2 and GBF3 to bind DNA as heterodimers. Mutagenesis of the leucine zipper of GBF4 indicates that the mutation of a single amino acid confers upon the protein the ability to recognize the G-box as a homodimer, apparently by altering the charge distribution within the leucine zipper.
Mesh Terms:
Amino Acid Sequence, Arabidopsis, Base Sequence, Basic-Leucine Zipper Transcription Factors, DNA Mutational Analysis, DNA-Binding Proteins, G-Box Binding Factors, Genes, Plant, Leucine Zippers, Molecular Sequence Data, Multigene Family, Oncogene Protein p65(gag-jun), Oncogene Proteins v-fos, Protein Conformation, Sequence Homology, Amino Acid, Transcription Factors
Amino Acid Sequence, Arabidopsis, Base Sequence, Basic-Leucine Zipper Transcription Factors, DNA Mutational Analysis, DNA-Binding Proteins, G-Box Binding Factors, Genes, Plant, Leucine Zippers, Molecular Sequence Data, Multigene Family, Oncogene Protein p65(gag-jun), Oncogene Proteins v-fos, Protein Conformation, Sequence Homology, Amino Acid, Transcription Factors
Proc. Natl. Acad. Sci. U.S.A.
Date: Mar. 29, 1994
PubMed ID: 8146148
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