Nucleic Acids Research Advance Access originally published online on December 17, 2007
Nucleic Acids Research 2008 36(3):915-928; doi:10.1093/nar/gkm1114
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Nucleic Acids Research, 2008, Vol. 36, No. 3 915-928
© 2007 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.
Molecular Biology |
Differentiation-dependent lysine 4 acetylation enhances MEF2C binding to DNA in skeletal muscle cells
1Department of Biomedical Sciences, University of Modena and Reggio Emilia, Modena and 2Mass Spectrometry Unit, DIBIT San Raffaele Scientific Institute, Milano, Italy
*To whom correspondence should be addressed. Tel: +39 059 2055403; Fax: +39 059 2055410; Email: susanna.molinari{at}unimore.it
Correspondence may also be addressed to Stefano Ferrari. Tel: +39 059 2055403; Fax: +39 059 2055410; Email: stefano.ferrari{at}unimore.it
Received August 17, 2007. Revised November 9, 2007. Accepted November 28, 2007.
Myocyte enhancer factor 2 (MEF2) proteins play a key role in promoting the expression of muscle-specific genes in differentiated muscle cells. MEF2 activity is regulated by the association with several transcriptional co-factors and by post-translational modifications. In the present report, we provide evidence for a novel regulatory mechanism of MEF2C activity, which occurs at the onset of skeletal muscle differentiation and is based on Lys4 acetylation. This covalent modification results in the enhancement of MEF2C binding to DNA and chromatin. In particular, we report that the kinetic parameters of MEF2/DNA association change substantially upon induction of differentiation to give a more stable complex and that this effect is mediated by Lys4 acetylation. We also show that Lys4 acetylation plays a prominent role in the p300-dependent activation of MEF2C.
Present address: Daniela Ferrari, Center for Hemochromatosis, Department of Internal Medicine, University of Modena and Reggio Emilia, Modena, Italy
The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors
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