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.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
Dallas PB,Cheney IW,Liao DW,Bowrin V,Byam W,Pacchione S,Kobayashi R,Yaciuk P,Moran Edoi
10.1128/mcb.18.6.3596subject
Has Abstractpub_date
1998-06-01 00:00:00pages
3596-603issue
6eissn
0270-7306issn
1098-5549journal_volume
18pub_type
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