21 research outputs found
Ash2 acts as an Ecdysone Receptor coactivator by stabilizing the histone methyltransferase Trr.
Get PDFThe molting hormone ecdysone triggers chromatin changes via histone modifica- tions 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 tran- scriptional 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 ecdy- sone-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 re- quired for its stabilization. Thus we propose that Ash2 functions together with Trr as an ecdysone receptor coactivator
Excisive recombination of the SLP1 element in Streptomyces lividans is mediated by Int and enhanced by Xis
No full textA plasmid from the methylotrophic actinomycete Amycolatopsis methanolica capable of site-specific integration
No full textHigh level transactivation by the ecdysone receptor complex at the core recognition motif
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Cloning of Frankia species putative tRNA(Pro) genes and their efficacy for pSAM2 site-specific integration in Streptomyces lividans
No full textOrganization and copy number of initiator tRNA genes in slow- and fast-growing mycobacteria
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The palindromic DNA-bound USP/EcR nuclear receptor adopts an asymmetric organization with allosteric domain positioning
No full textMolecular Cloning, Characterization, and Expression Pattern of the Ultraspiracle Gene Homolog (RXR/USP) from the Hemimetabolous Insect Periplaneta americana (Dictyoptera, Blattidae) During Vitellogenesis
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