Open Accessp300/CREB Binding Protein-Related Protein p270 Is a Component of Mammalian SWI/SNF Complexes
Author(s) -
Peter B. Dallas,
I.W. Cheney,
Da Wei Liao,
Valerie Bowrin,
Whitney Byam,
Stephen Pacchione,
Ryûji Kobayashi,
Peter Yaciuk,
Elizabeth Morán
Publication year - 1998
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.18.6.3596
Subject(s) - biology , creb binding protein , creb , microbiology and biotechnology , p300 cbp transcription factors , dna binding protein , nuclear protein , transcription factor , swi/snf , chromatin , histone , tata binding protein , transcription (linguistics) , chromatin remodeling , biochemistry , histone acetyltransferases , dna , gene , linguistics , philosophy
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.