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ABSTRACT
p300 and the closely related CREB binding protein (CBP) are transcriptional adaptors that are present in intracellular complexes with TATA binding protein (TBP) and bind to upstream activators including p53 and nuclear hormone receptors. They have intrinsic and associated histone acetyltransferase activity, suggesting that chromatin modification is an essential part of their role in regulating transcription. Detailed characterization of a panel of antibodies raised against p300/CBP has revealed the existence of a 270-kDa cellular protein, p270, distinct from p300 and CBP but sharing at least two independent epitopes with p300. The subset of p300/CBP-derived antibodies that cross-reacts with p270 consistently coprecipitates a series a cellular proteins with relative molecular masses ranging from 44 to 190 kDa. Purification and analysis of various proteins in this group reveals that they are components of the human SWI/SNF complex and that p270 is an integral member of this complex.
ACKNOWLEDGMENTS
The first three authors contributed equally to this work.
We thank Gerry Crabtree, Nouria Hernandez, and Ed Harlow for generous gifts of antibodies, and we thank Annette Heagy, Patty Baxter, Steve Dorfman, and John Gibas for expert technical assistance.
This work was supported by PHS grants CA53592, CA55330 (E.M.), and CA68066 (P.Y.) from the NIH.