Like certain protein kinases, some protein acetyltransferases such as p300 may use an inhibitory loop that can be regulated to limit the accessibility of substrates to its active site. The finding that autoacetylation of this loop activates the acetyltransferase provides the first evidence for an acetylation cascade analogous to protein kinase cascades.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 12 print issues and online access
$189.00 per year
only $15.75 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
References
Marmorstein, R. & Roth, S.Y. Curr. Opin. Genet. Dev. 11, 155–161 (2001).
Thompson, P.R. et al. Nat. Struct. Mol. Biol. 11, 308–315 (2004).
Adams, J.A. Biochemistry 42, 601–607 (2003).
Hubbard, S.R. EMBO J. 16, 5572–5581 (1997).
Johnson, L.N., Noble, M.E. & Owen, D.J. Cell 85, 149–158 (1996).
Morgan, D.O. Nature 374, 131–134 (1995).
Marmorstein, R. J. Mol. Biol. 311, 433–444 (2001).
Kouzarides, T. EMBO J. 19, 1176–1179 (2000).
Acknowledgements
I thank J. Adams for advice and S. Tan for generating the structures in Figure 1. Research support comes from the US National Institutes of Health (GM059055).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Pugh, B. Is acetylation the key to opening locked gates?. Nat Struct Mol Biol 11, 298–300 (2004). https://doi.org/10.1038/nsmb0404-298
Issue Date:
DOI: https://doi.org/10.1038/nsmb0404-298
