
pmid: 9070273
In screening for proteins that interact with the basic zipper (bZip) transcription factor, c-Maf, we isolated USF2/FIP. USF2 is a member of the bHLH-Zip protein family, possessing a basic (b) DNA binding region, a helix-loop-helix (HLH) motif, and a leucine zipper (Zip) structure. Mutants of USF2 that lacked a Zip formed heterodimers with c-Maf, but did not homodimerize. Deletion of the USF2 basic region or mutation of its helices abrogated its binding to c-Maf, but had no effect on homodimerization. A functional c-Maf bZip motif was necessary for both homodimerization and heterodimerization with USF2. These data suggest a tetrameric configuration for Maf-USF2 complexes. In the presence of USF2, the DNA binding activity of c-Maf was markedly reduced. Therefore, USF2 and c-Maf may interact to regulate gene expression.
Leucine Zippers, Binding Sites, Kainic Acid, Helix-Loop-Helix Motifs, Nerve Tissue Proteins, Recombinant Proteins, DNA-Binding Proteins, Basic-Leucine Zipper Transcription Factors, Biopolymers, G-Box Binding Factors, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-maf, Upstream Stimulatory Factors, Cycloheximide, Promoter Regions, Genetic, Protein Binding, Transcription Factors
Leucine Zippers, Binding Sites, Kainic Acid, Helix-Loop-Helix Motifs, Nerve Tissue Proteins, Recombinant Proteins, DNA-Binding Proteins, Basic-Leucine Zipper Transcription Factors, Biopolymers, G-Box Binding Factors, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-maf, Upstream Stimulatory Factors, Cycloheximide, Promoter Regions, Genetic, Protein Binding, Transcription Factors
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