PubMed:7809597 JSONTXT

{"project":"AIMed","denotations":[{"id":"T1","span":{"begin":0,"end":3},"obj":"protein"},{"id":"T2","span":{"begin":56,"end":63},"obj":"protein"},{"id":"T3","span":{"begin":68,"end":75},"obj":"protein"},{"id":"T4","span":{"begin":106,"end":109},"obj":"protein"},{"id":"T5","span":{"begin":236,"end":260},"obj":"protein"},{"id":"T6","span":{"begin":262,"end":267},"obj":"protein"},{"id":"T7","span":{"begin":410,"end":413},"obj":"protein"},{"id":"T8","span":{"begin":438,"end":443},"obj":"protein"},{"id":"T9","span":{"begin":453,"end":460},"obj":"protein"},{"id":"T10","span":{"begin":465,"end":472},"obj":"protein"},{"id":"T11","span":{"begin":539,"end":542},"obj":"protein"},{"id":"T12","span":{"begin":660,"end":667},"obj":"protein"},{"id":"T13","span":{"begin":672,"end":679},"obj":"protein"},{"id":"T14","span":{"begin":704,"end":709},"obj":"protein"},{"id":"T15","span":{"begin":740,"end":760},"obj":"protein"},{"id":"T16","span":{"begin":762,"end":766},"obj":"protein"},{"id":"T17","span":{"begin":775,"end":783},"obj":"protein"},{"id":"T18","span":{"begin":785,"end":793},"obj":"protein"},{"id":"T19","span":{"begin":799,"end":807},"obj":"protein"},{"id":"T20","span":{"begin":876,"end":879},"obj":"protein"},{"id":"T21","span":{"begin":904,"end":911},"obj":"protein"},{"id":"T22","span":{"begin":916,"end":923},"obj":"protein"},{"id":"T23","span":{"begin":970,"end":977},"obj":"protein"},{"id":"T24","span":{"begin":982,"end":989},"obj":"protein"},{"id":"T25","span":{"begin":1056,"end":1059},"obj":"protein"}],"text":"p53 transcriptional activation mediated by coactivators TAFII40 and TAFII60.\nThe tumor suppressor protein p53 is a transcriptional regulator that enhances the expression of proteins that control cellular proliferation. The multisubunit transcription factor IID (TFIID) is thought to be a primary target for site-specific activators of transcription. Here, a direct interaction between the activation domain of p53 and two subunits of the TFIID complex, TAFII40 and TAFII60, is reported. A double point mutation in the activation domain of p53 impaired the ability of this domain to activate transcription and, simultaneously, its ability to interact with both TAFII40 and TAFII60. Furthermore, a partial TFIID complex containing Drosophila TATA binding protein (dTBP), human TAFII250, dTAFII60, and dTAFII40 supported activation by a Gal4-p53 fusion protein in vitro, whereas TBP or a subcomplex lacking TAFII40 and TAFII60 did not. Together, these results suggest that TAFII40 and TAFII60 are important targets for transmitting activation signals between p53 and the initiation complex."}