scholarly journals Histone-Binding Protein RBBP4

2020 ◽  
Author(s):  
2013 ◽  
Vol 5 (200) ◽  
pp. 200ra115-200ra115 ◽  
Author(s):  
E. Pavlopoulos ◽  
S. Jones ◽  
S. Kosmidis ◽  
M. Close ◽  
C. Kim ◽  
...  

2019 ◽  
Vol 10 ◽  
Author(s):  
Jiyu Ju ◽  
Jia Xu ◽  
Yaoqiang Zhu ◽  
Xiaoyan Fu ◽  
Laurence Morel ◽  
...  

The Testis ◽  
2000 ◽  
pp. 143-150 ◽  
Author(s):  
Michael G. O’Rand ◽  
Iglika N. Batova ◽  
Richard T. Richardson

2002 ◽  
Vol 278 (10) ◽  
pp. 8846-8852 ◽  
Author(s):  
Oleg M. Alekseev ◽  
David C. Bencic ◽  
Richard T. Richardson ◽  
Esther E. Widgren ◽  
Michael G. O'Rand

2006 ◽  
Vol 115 (1) ◽  
pp. 10-15 ◽  
Author(s):  
S. Kobayashi ◽  
S. Uchiyama ◽  
T. Sone ◽  
M. Noda ◽  
L. Lin ◽  
...  

2000 ◽  
Vol 20 (14) ◽  
pp. 4970-4978 ◽  
Author(s):  
Qinghong Zhang ◽  
Ngan Vo ◽  
Richard H. Goodman

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 glutathioneS-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 theKm 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.


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