Functional and physical associations between NF-kappa B and C/EBP family members: a Rel domain-bZIP interaction.

作者: B Stein , P C Cogswell , A S Baldwin

DOI: 10.1128/MCB.13.7.3964

关键词: BiologyB vitaminsEnhancerBinding siteRel homology domainDNA-binding proteinLeucine zipperCcaat-enhancer-binding proteinsPromoterMolecular biology

摘要: NF-kappa B and C/EBP represent distinct families of transcription factors that target unique DNA enhancer elements. The heterodimeric complex is composed two subunits, a 50- 65-kDa protein. All members the family, including product proto-oncogene c-rel, are characterized by their highly homologous approximately 300-amino-acid N-terminal region. This Rel homology domain mediates binding, dimerization, nuclear targeting these proteins. contains bZIP region, which motifs in C-terminal half protein: basic region involved binding leucine zipper motif dimerization. family consist several related proteins, alpha, beta, gamma, delta, form homodimers heterodimers with each other. We now demonstrated unexpected cross-coupling three family. p65, p50, functionally synergize delta. results inhibition promoters kappa synergistic stimulation sites. These studies demonstrate augments gene expression mediated multimerized c-fos serum response element presence C/EBP. show direct physical association B. highlights mechanism regulation involving an interaction between factor families.

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