Nucleic Acids Research Advance Access originally published online on March 20, 2009
Nucleic Acids Research 2009 37(9):2996-3006; doi:10.1093/nar/gkp163
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Nucleic Acids Research, 2009, Vol. 37, No. 9 2996-3006
© 2009 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Gene Regulation, Chromatin and Epigenetics |
The transcriptional coactivator MAML1 regulates p300 autoacetylation and HAT activity
cibor11Department of Biosciences and Nutrition, Karolinska Institutet, 141 86 Stockholm, Sweden and 2Department of Pharmacology and Molecular Sciences, Johns Hopkins School of Medicine, Baltimore, MD 21205, USA
*To whom correspondence should be addressed. Tel: +46 8 58583951; Fax: +46 8 7116659; Email: annika.wallberg{at}ki.se
Received October 13, 2008. Revised February 26, 2009. Accepted February 27, 2009.
MAML1 is a transcriptional coregulator originally identified as a Notch coactivator. MAML1 is also reported to interact with other coregulator proteins, such as CDK8 and p300, to modulate the activity of Notch. We, and others, previously showed that MAML1 recruits p300 to Notch-regulated genes through direct interactions with the DNA–CSL–Notch complex and p300. MAML1 interacts with the C/H3 domain of p300, and the p300–MAML1 complex specifically acetylates lysines of histone H3 and H4 tails in chromatin in vitro. In this report, we show that MAML1 potentiates p300 autoacetylation and p300 transcriptional activation. MAML1 directly enhances p300 HAT activity, and this coincides with the translocation of MAML1, p300 and acetylated histones to nuclear bodies.
The authors wish it to be known that, in their opinion, the second and third authors should be regarded as joint Second Authors.
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