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p300/CBP proteins: HATs for transcriptional bridges and scaffolds

Ho Man Chan and Nicholas B. La Thangue*

Division of Biochemistry and Molecular Biology, Davidson Building, University of Glasgow, Glasgow, G12 8QQ, UK



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  		Fig. 1. Organisation of p300/CBP proteins. (A) Comparison of p300 and CBP. The dark regions indicate the areas of highest homology, with the percentage amino acid identity between the two proteins indicated. The size of each protein, in number of amino acid residues, is indicated. (B) The functional domains in p300 are indicated, including the cysteine/histidine-rich domains CH1, CH2 and CH3, the KIX domain, the bromodomain (Br) and the ADA2 homology region. The N- and C-terminal domains of p300/CBP can act as transactivation domains, and the acetyl-transferase domain is located in the central region of the protein. The regions that have been shown to bind to target proteins, together with the identity of the interacting proteins, are shown.

 


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  		Fig. 2. Role of p300/CBP during cell cycle progression. The diagram describes the role of p300 in regulating the activity of the cell cycle transcription factor E2F. Phosphorylation of pRb by cyclin-D-CDK4 kinase releases pRb from E2F, thereafter facilitating the activation of E2F-target genes. Subsequent phosphorylation of a CDK site by cyclin-E-CDK2 in the transactivation domain of E2F augments the interaction with p300, thereafter leading to the increased transcriptional activity of E2F-target genes.

 


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  		Fig. 3. Mechanisms of transcriptional activation by p300/CBP. (A) In the bridging model, p300/CBP proteins connect sequence-specific transcription factors to the transcription apparatus. (B) In the scaffold model, p300/CBP act as a protein scaffold for the assembly of multicomponent complexes that confer transcriptional activation. Examples of possible components, such as HAT (a co-factor containing acetyl-transferase activity), JMY and NAP, are indicated. (C) In the HAT model, either the intrinsic HAT activity of p300/CBP or HATs assembled in multicomponent complexes target chromatin and/or transcription factors to facilitate a transcriptional response.

 

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© The Company of Biologists Ltd 2001