This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Gamper, A. M.
Right arrow Articles by Roeder, R. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gamper, A. M.
Right arrow Articles by Roeder, R. G.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, April 2008, p. 2517-2527, Vol. 28, No. 8
0270-7306/08/$08.00+0     doi:10.1128/MCB.01461-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Multivalent Binding of p53 to the STAGA Complex Mediates Coactivator Recruitment after UV Damage{triangledown}

Armin M. Gamper and Robert G. Roeder*

Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, New York 10021

Received 13 August 2007/ Returned for modification 22 October 2007/ Accepted 28 January 2008

The recruitment of transcriptional coactivators, including histone modifying enzymes, is an important step in transcription regulation. A typical activator is thought to interact with several cofactors, presumably in a sequential manner. The common use of several cofactors raises the question of how activators achieve both cofactor selectivity and diversity. Human STAGA is a multiprotein complex with the acetyltransferase GCN5L as the catalytic subunit. Here, we first show, through RNA interference-mediated knock-down and chromatin immunoprecipitation assays, that GCN5 plays a role in p53-dependent gene activation. We then employ p53 mutagenesis, in vitro binding, protein-protein cross-linking, and chromatin immunoprecipitation assays to establish a novel role for the second p53 activation subdomain (AD2) in STAGA recruitment and, further, to demonstrate that optimal binding of STAGA to p53 involves interactions of STAGA subunits TAF9, GCN5, and ADA2b, respectively, with AD1, AD2, and carboxy-terminal domains of p53. These results provide concrete evidence for mediation of transcription factor binding to coactivator complexes through multiple interactions. Based on our data, we propose a cooperative and modular binding mode for the recruitment of coactivator complexes to promoters.

* Corresponding author. Mailing address: Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, NY 10021. Phone: (212) 327-7600. Fax: (212) 327-7949. E-mail: roeder{at}mail.rockefeller.edu

{triangledown} Published ahead of print on 4 February 2008.

Molecular and Cellular Biology, April 2008, p. 2517-2527, Vol. 28, No. 8
0270-7306/08/$08.00+0     doi:10.1128/MCB.01461-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Ferreon, J. C., Lee, C. W., Arai, M., Martinez-Yamout, M. A., Dyson, H. J., Wright, P. E. (2009). Cooperative regulation of p53 by modulation of ternary complex formation with CBP/p300 and HDM2. Proc. Natl. Acad. Sci. USA 106: 6591-6596 [Abstract] [Full Text]  
  • Gamper, A. M., Kim, J., Roeder, R. G. (2009). The STAGA Subunit ADA2b Is an Important Regulator of Human GCN5 Catalysis. Mol. Cell. Biol. 29: 266-280 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»