Journal ArticleDOI
The CBP co-activator is a histone acetyltransferase
TLDR
It is shown that CBP has intrinsic HAT activity, and Targeting CBP-associated H AT activity to specific promoters may be a mechanism by which E1A acts as a transcriptional activator.Abstract:
The CBP protein acts as a transcriptional adaptor for many different transcription factors by directly contacting DNA-bound activators. One mechanism by which CBP is thought to stimulate transcription is by recruiting the histone acetyltransferase (HAT) P/CAF to the promoter. Here we show that CBP has intrinsic HAT activity. The HAT domain of CBP is adjacent to the binding site for the transcriptional activator E1A. Although E1A displaces P/CAF from CBP, it does not disrupt the CBP-associated HAT activity. Thus E1A carries HAT activity when complexed with CBP. Targeting CBP-associated HAT activity to specific promoters may therefore be a mechanism by which E1A acts as a transcriptional activator.read more
Citations
More filters
Journal ArticleDOI
A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis.
Pere Puigserver,Zhidan Wu,Cheol Won Park,Reed A. Graves,Margaret E. Wright,Bruce M. Spiegelman +5 more
TL;DR: Results indicate that PGC-1 plays a key role in linking nuclear receptors to the transcriptional program of adaptive thermogenesis.
Journal ArticleDOI
Peroxisome proliferator-activated receptors: nuclear control of metabolism.
Béatrice Desvergne,Walter Wahli +1 more
TL;DR: This work has shown that direct expression of PPAR mRNAs in the absence of a specific carrier gene results in down-regulation in the activity of other PPARs, and these properties are consistent with those of a “spatially aggregating substance”.
Journal ArticleDOI
Histone acetylation in chromatin structure and transcription
TL;DR: The amino termini of histones extend from the nucleosomal core and are modified by acetyltransferases and deacetylases during the cell cycle, which may direct histone assembly and help regulate the unfolding and activity of genes.
Journal ArticleDOI
Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain.
Andrew J. Bannister,Philip Zegerman,Janet F. Partridge,Eric A. Miska,Jean O. Thomas,Robin C. Allshire,Tony Kouzarides +6 more
TL;DR: A stepwise model for the formation of a transcriptionally silent heterochromatin is provided: SUV39H1 places a ‘methyl marker’ on histone H3, which is then recognized by HP1 through its chromo domain, which may also explain the stable inheritance of theheterochromatic state.
Journal ArticleDOI
Activation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain
Wei Gu,Robert G. Roeder +1 more
TL;DR: It is demonstrated that p53 can be modified by acetylated both in vivo and in vitro, indicating a novel pathway for p53 activation and providing an example of an acetylation-mediated change in the function of a nonhistone regulatory protein.
References
More filters
Journal ArticleDOI
Phosphorylated CREB binds specifically to the nuclear protein CBP
John C. Chrivia,Roland P. S. Kwok,Ned J.C. Lamb,Masatoshi Hagiwara,Marc Montminy,Richard H. Goodman +5 more
TL;DR: It is proposed that CBP may participate in cAMP-regulated gene expression by interacting with the activated phosphorylated form of CREB, which is activated as a result of phosphorylation by protein kinase A7.
Journal ArticleDOI
A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
Xiang Jiao Yang,Vasily Ogryzko,Jun-ichi Nishikawa,Jun-ichi Nishikawa,Bruce H. Howard,Yoshihiro Nakatani +5 more
TL;DR: A new cellular p300/CBP-associated factor (P/CAF) having intrinsic histone acetylase activity has been identified that competes with E1A, a new adenoviral oncoprotein that induces progression through the cell cycle by binding to the products of the p300 and retinoblastoma gene families.
Journal ArticleDOI
Role of CBP/P300 in nuclear receptor signalling
Debabrata Chakravarti,Vickie J. LaMorte,Michael C. Nelson,Toshihiro Nakajima,Ira G. Schulman,Henry Juguilon,Marc Montminy,Ronald M. Evans +7 more
TL;DR: In vitro and in vivo evidence is provided that identifies the CREB-binding protein (CBP) and its homologue P300 as cofactors mediating nuclear-receptor-activated gene transcription and may serve as integrators of extracellular and intracellular signalling pathways.
Journal ArticleDOI
CBP-induced stimulation of c-Fos activity is abrogated by E1A.
TL;DR: A model whereby E1A can modulate AP1 activity by directly competing for the CBP co‐activator protein is supported by a model whereby CBP binds c‐Fos in a phosphorylation‐independent manner in vitro, using a domain distinct from that required to bind CREB.
Journal ArticleDOI
Human p300 Protein Is a Coactivator for the Transcription Factor MyoD
TL;DR: It is shown that the repression of MyoD-mediated E box (MyoD consensus) reporter activity by E1A is correlated with its interaction with p300, indicating that p300 participates in Myo D-dependent transactivation.