PubMed:7685215 JSONTXT

{"project":"AIMed","denotations":[{"id":"T1","span":{"begin":20,"end":23},"obj":"protein"},{"id":"T2","span":{"begin":28,"end":31},"obj":"protein"},{"id":"T3","span":{"begin":72,"end":96},"obj":"protein"},{"id":"T4","span":{"begin":98,"end":101},"obj":"protein"},{"id":"T5","span":{"begin":106,"end":109},"obj":"protein"},{"id":"T6","span":{"begin":422,"end":427},"obj":"protein"},{"id":"T7","span":{"begin":432,"end":437},"obj":"protein"},{"id":"T8","span":{"begin":477,"end":501},"obj":"protein"},{"id":"T9","span":{"begin":503,"end":506},"obj":"protein"},{"id":"T10","span":{"begin":712,"end":717},"obj":"protein"},{"id":"T11","span":{"begin":722,"end":727},"obj":"protein"},{"id":"T12","span":{"begin":760,"end":763},"obj":"protein"},{"id":"T13","span":{"begin":855,"end":860},"obj":"protein"},{"id":"T14","span":{"begin":865,"end":870},"obj":"protein"},{"id":"T15","span":{"begin":928,"end":931},"obj":"protein"},{"id":"T16","span":{"begin":993,"end":996},"obj":"protein"},{"id":"T17","span":{"begin":1070,"end":1073},"obj":"protein"},{"id":"T18","span":{"begin":1090,"end":1095},"obj":"protein"},{"id":"T19","span":{"begin":1100,"end":1105},"obj":"protein"},{"id":"T20","span":{"begin":1132,"end":1137},"obj":"protein"},{"id":"T21","span":{"begin":1142,"end":1147},"obj":"protein"},{"id":"T22","span":{"begin":1219,"end":1222},"obj":"protein"}],"text":"The bZIP domains of Fos and Jun mediate a physical association with the TATA box-binding protein.\nFos 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 indirect 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 protein (TBP), the general transcription factor required for initiating the assembly of transcription complexes, was investigated. Using co-immunoprecipitation 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."}