Histone binding protein RbAp48 interacts with a complex of CREB binding protein and phosphorylated CREB

Qinghong Zhang, Ngan Vo, Richard Goodman

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

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 K(m) 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.

Original languageEnglish (US)
Pages (from-to)4970-4978
Number of pages9
JournalMolecular and Cellular Biology
Volume20
Issue number14
DOIs
StatePublished - Jul 2000

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CREB-Binding Protein
Histones
Carrier Proteins
Acetylation
Retinoblastoma-Binding Protein 4
Histone Acetyltransferases
Cell Extracts
Glutathione Transferase
Gene Library
HeLa Cells
Protein Binding
Transcriptional Activation
Embryonic Structures
Yeasts

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Histone binding protein RbAp48 interacts with a complex of CREB binding protein and phosphorylated CREB. / Zhang, Qinghong; Vo, Ngan; Goodman, Richard.

In: Molecular and Cellular Biology, Vol. 20, No. 14, 07.2000, p. 4970-4978.

Research output: Contribution to journalArticle

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