The bZIP domains of Fos and Jun mediate a physical association with the TATA box-binding protein
Fos and Jun oncoproteins form a complex that regulates transcription from promoters containing AP-1 binding sites. These two proteins, like other transcriptional activators, are likely to stimulate transcription through direct and/or in direct interactions with members of the basal transcriptional machinery. The ability of c-Fos and c-Jun proteins to interact directly with the TATA box-binding prote in (TBP), the general transcription factor required for initiating the assembly of transcription complexes, was investigated. Using co-immunopre cipitation and protein -protein association assays, we show that both c-Fos and c-Jun bind specifically and stably to TBP. Mutational analysis demonstrates that both the basic region and leucine zipper domains of c-Fos and c-Jun are necessary and sufficient for stable association with TBP. A 51-residue region from the conserved C-terminal region of TBP, previously shown to be the binding site for the viral activator protein E1A, interacts with c-Fos and c-Jun proteins. We propose that c-Fos and c-Jun proteins function as transcriptional activators, in part by recruiting TBP to form complexes to initiate RNA synthesis.
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Document Type: Research Article
Publication date: January 1, 1993
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