Document Type
Article
Publication Date
1-1-2013
Abstract
The molting hormone ecdysone triggers chromatin changes via histone modifications that are important for gene regulation. On hormone activation, the ecdysone receptor (EcR) binds to the SET domain-containing histone H3 methyltransferase trithorax-related protein (Trr). Methylation of histone H3 at lysine 4 (H3K4me), which is associated with transcriptional activation, requires several cofactors, including Ash2. We find that ash2 mutants have severe defects in pupariation and metamorphosis due to a lack of activation of ecdysone-responsive genes. This transcriptional defect is caused by the absence of the H3K4me3 marks set by Trr in these genes. We present evidence that Ash2 interacts with Trr and is required for its stabilization. Thus we propose that Ash2 functions together with Trr as an ecdysone receptor coactivator.
Recommended Citation
Carbonell, Albert; Mazo, Alexander; Serras, Florenci; and Corominas, Montserrat, "Ash2 acts as an ecdysone receptor coactivator by stabilizing the histone methyltransferase Trr." (2013). Department of Biochemistry and Molecular Biology Faculty Papers. Paper 54.
https://jdc.jefferson.edu/bmpfp/54
PubMed ID
23197473
Comments
This article has been peer reviewed and is published in Molecular Biology of the Cell Volume 24, Issue 3, 1 January 2013, Pages 361-372. The published version is available at DOI: 10.1091/mbc.E12-04-0267. © 2013 Jo et al.