Related Experiment Video
Updated: May 16, 2026

An Acetyl-Click Chemistry Assay to Measure Histone Acetyltransferase 1 Acetylation
Published on: January 26, 2024
Ash2 acts as an ecdysone receptor coactivator by stabilizing the histone methyltransferase Trr
Albert Carbonell1, Alexander Mazo, Florenci Serras
1Departament de Genètica and Institut de Biomedicina, Universitat de Barcelona, 08028 Barcelona, Spain.
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.
Related Concept Videos
Co-activators and Co-repressors
Co-activators and Co-repressors
Master Transcription Regulators
Master Transcription Regulators
Spreading of Chromatin Modifications
Writers
The writer is an enzyme that can...
Histone Modification
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...

