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Molecular and Cellular Biology, July 2000, p. 4970-4978, Vol. 20, No. 14
Vollum Institute, Oregon Health Sciences
University, Portland, Oregon
Received 7 December 1999/Returned for modification 13 January
2000/Accepted 24 April 2000
A CREB-CREB binding protein (CBP) complex was used as bait to
screen a mouse embryo cDNA library in yeast. One of the strongest interactions identified the histone binding protein RbAp48. RbAp48 also
interacted weakly with CBP alone but did not interact with phosphorylated or nonphosphorylated CREB. CBP (or its homologue p300)
from HeLa cell nuclear extracts coimmunoprecipitated with RbAp48 and
its homologue RbAp46 and bound to a glutathione
S-transferase-RbAp48 fusion protein. This interaction was
stimulated by the addition of phosphorylated CREB and allowed the
association of core histones and mononucleosomes in an
acetylation-dependent manner. RbAp48 lowered the
Km of CBP histone acetylase activity and
facilitated p300-mediated in vitro transcription of a chromatinized
template in the presence of acetylcoenzyme A. These data indicate that the association of phosphorylated CREB with CBP promotes the binding of
RbAp48 and its homologue RbAp46, allowing the formation of a complex
that facilitates histone acetylation during transcriptional activation.
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Histone Binding Protein RbAp48 Interacts with a
Complex of CREB Binding Protein and Phosphorylated CREB
*
Corresponding author. Mailing address: Vollum
Institute, Oregon Health Sciences University, 3181 S.W. Sam Jackson
Park Rd., Portland, OR 97201. Phone: (503) 494-5078. Fax: (503)
494-4353. E-mail: goodmanr{at}ohsu.edu.
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