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Mol Cell Biol, June 1998, p. 3596-3603, Vol. 18, No. 6
Fels Institute for Cancer Research and
Molecular Biology, Temple University School of Medicine, Philadelphia,
Pennsylvania 191401;
Cold Spring Harbor
Laboratory, Cold Spring Harbor, New York
117242; and
St. Louis University
School of Medicine, St. Louis, Missouri 631043
Received 14 August 1997/Returned for modification 2 October
1997/Accepted 11 March 1998
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.
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
p300/CREB Binding Protein-Related Protein p270 Is a Component
of Mammalian SWI/SNF Complexes

*
Corresponding author. Mailing address: Fels Institute
for Cancer Research and Molecular Biology, Temple University School of
Medicine, 3307 N. Broad St., Philadelphia, PA 19140. Phone: (215)
707-7313. Fax: (215) 707-6989. E-mail:
betty{at}sgi1.fels.temple.edu.
Present address: Canji, Inc., San Diego, CA 92121.
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