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Structural features of human histone acetyltransferase p300 and its complex with p53

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Title Structural features of human histone acetyltransferase p300 and its complex with p53
 
Creator Banerjee, Siddhartha
M, Arif
Rakshit, Tatini
Roy, Neeladri Sekhar
Kundu, Tapas K
Roy, Siddhartha
Mukhopadhyay, Rupa
 
Subject Structural Biology & Bioinformatics
 
Description The protein p300 is a multifunctional transcriptional coactivator that plays pivotal role in several cellular functions. Although structures of several domains have been solved in isolation, the structures of full-length protein (p300 FL) or its complexes with transcription activators are completely unknown. Herein, we applied atomic force microscopy to visualize p300 FL. We found that it is
almost prolate ellipsoidal in shape, having several bulges. We further identified the functionally significant
N-terminal and C-terminal regions, by applying domain-specific antibodies and found that they are located near one end and centre of the molecule, respectively. Importantly, we have visualized the complex between p300 FL and tumor suppressor protein p53. The relevance of these data in understanding dynamics of p300 during acetylation and transcription will be mentioned.
 
Publisher Elsevier
 
Date 2012
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/2274/1/FEBS_LETTERS__V._586_(_21)_3793%2D3798_;2012.pdf
Banerjee, Siddhartha and M, Arif and Rakshit, Tatini and Roy, Neeladri Sekhar and Kundu, Tapas K and Roy, Siddhartha and Mukhopadhyay, Rupa (2012) Structural features of human histone acetyltransferase p300 and its complex with p53. FEBS Letters, 586 (21). pp. 3793-3798.
 
Relation http://dx.doi.org/10.1016/j.febslet.2012.09.012
http://www.eprints.iicb.res.in/2274/