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Regulation of the p300 HAT domain via a novel activation loop
Nature Structural and Molecular Biology
  • Paul R. Thompson
  • Dongxia Wang
  • Marcella Fulco
  • Natalia Pediconi
  • Dianzheng Zhang, Philadelphia College of Osteopathic Medicine
  • Woojin An
  • Qingyuan Ge
  • Robert R. Roeder
  • Jiemin Wong
  • Massimo Levrero
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Publication Date
The transcriptional coactivator p300 is a histone acetyltransferase (HAT) whose function is critical for regulating gene expression in mammalian cells. However, the molecular events that regulate p300 HAT activity are poorly understood. We evaluated autoacetylation of the p300 HAT protein domain to determine its function. Using expressed protein ligation, the p300 HAT protein domain was generated in hypoacetylated form and found to have reduced catalytic activity. This basal catalytic rate was stimulated by autoacetylation of several key lysine sites within an apparent activation loop motif. This post-translational modification and catalytic regulation of p300 HAT activity is conceptually analogous to the activation of most protein kinases by autophosphorylation. We therefore propose that this autoregulatory loop could influence the impact of p300 on a wide variety of signaling and transcriptional events.

This article was published in Nature Structural and Molecular Biology, Volume 11, Issue 4, Pages 308-315.

The published version is available at

Copyright © 2004 Nature Publishing Group.

Citation Information
Paul R. Thompson, Dongxia Wang, Marcella Fulco, Natalia Pediconi, et al.. "Regulation of the p300 HAT domain via a novel activation loop" Nature Structural and Molecular Biology Vol. 11 Iss. 4 (2004) p. 308 - 315
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