Nucleic Acids Research Advance Access originally published online on January 31, 2007
Nucleic Acids Research 2007 35(4):1312-1321; doi:10.1093/nar/gkm038
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Nucleic Acids Research, 2007, Vol. 35, No. 4 1312-1321
© 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 |
ATF2 is required for amino acid-regulated transcription by orchestrating specific histone acetylation
1UMR 1019, Unité de Nutrition Humaine, INRA de Theix, 63122 Saint Genès Champanelle, France and 2Cell Regulation Laboratory, Paterson Institute for Cancer Research, Manchester, M204BX, UK
*To whom correspondence should be addressed. Tel: +33 4 73 62 41 50; Fax: +33 4 73 62 47 55; Email: bruhat{at}clermont.inra.fr Correspondence may also be addressed to Pierre Fafournoux. Tel: +33 4 73 62 45 62; Fax: +33 4 73 62 47 55; Email: fpierre{at}clermont.inra.fr
Received November 10, 2006. Revised January 6, 2007. Accepted January 8, 2007.
The transcriptional activation of CHOP (a CCAAT/enhancer-binding protein-related gene) by amino acid deprivation involves the activating transcription factor 2 (ATF2) and the activating transcription factor 4 (ATF4) binding the amino acid response element (AARE) within the promoter. Using a chromatin immunoprecipitation approach, we report that in vivo binding of phospho-ATF2 and ATF4 to CHOP AARE are associated with acetylation of histones H4 and H2B in response to amino acid starvation. A time course analysis reveals that ATF2 phosphorylation precedes histone acetylation, ATF4 binding and the increase in CHOP mRNA. We also show that ATF4 binding and histone acetylation are two independent events that are required for the CHOP induction upon amino acid starvation. Using ATF2-deficient mouse embryonic fibroblasts, we demonstrate that ATF2 is essential in the acetylation of histone H4 and H2B in vivo. The role of ATF2 on histone H4 acetylation is dependent on its binding to the AARE and can be extended to other amino acid regulated genes. Thus, ATF2 is involved in promoting the modification of the chromatin structure to enhance the transcription of a number of amino acid-regulated genes.
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