Different TBP-associated factors are required for mediating the stimulation of transcription in vitro by the acidic transactivator GAL-VP16 and the two nonacidic activation functions of the estrogen receptor.

AUTOR(ES)

Brou, C

RESUMO

The estrogen receptor (ER) contains two nonacidic transcriptional activation functions, AF-1 and AF-2 (formerly TAF-1 and TAF-2). In this study we show that AF-1 and AF-2 are able to stimulate transcription in vitro in a HeLa cell system when fused to the DNA binding domain of the yeast activator GAL4. We also demonstrate that a factor(s) required for the function of the ER AFs is chromatographically separable from a factor(s) necessary for the activity of the acidic activation domain of VP16. Moreover, immunoprecipitation experiments using a monoclonal antibody directed against the TATA box binding protein (TBP) indicate, that these different factors are associated with TBP in distinct TFIID complexes.

Documentos Relacionados

• The acidic transcriptional activator GAL-VP16 acts on preformed template-committed complexes.
• Evidence for a factor required for transcriptional stimulation by the chimeric acidic activator GAL-VP16 in HeLa cell extracts.
• The class II trans-activator CIITA interacts with the TBP-associated factor TAFII32.
• TBP-associated factors interact with DNA and govern species specificity of RNA polymerase I transcription.
• The yeast TATA-binding protein (TBP) core domain assembles with human TBP-associated factors into a functional TFIID complex.