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B with
TATA-binding Protein, Transcription Factor IIB, and Coactivators
(Received for publication, October 21, 1994; and in revised form, December 27, 1994)
We show that the transactivating COOH terminus of the p65
subunit of human transcription factor NF-
B directly binds the
general transcription factors TFIIB and TATA-binding protein (TBP) in vitro. Interaction of p65 with TFIIB required the most
COOH-terminal sequence repeat within TFIIB. A functional interaction of
TFIIB with p65 was evident from assays in yeast cells. Cotransfection
experiments in COS cells revealed that only overexpression of TBP was
able to further stimulate p65-dependent transactivation of a reporter
gene. The coexpression of neither TBP nor TFIIB was able to relieve
squelching, indicating the involvement of additional factors in
transactivation by p65. A cell-free assay using highly purified factors
revealed a specific transcriptional stimulation through the
COOH-terminal activation domain of NF-B by at least one cofactor,
PC1, isolated from HeLa cells. These data show that the potent acidic
transactivation domains in the COOH terminus of p65 are able to
functionally recruit various components of the basic transcription
machinery as well as coactivators.
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