Balance between Acetylation and Methylation of Histone H3 Lysine 9 on the E2F-Responsive Dihydrofolate Reductase Promoter

• DOI: 10.1128/mcb.23.5.1614-1622.2003
• Publication Date: 2003-02-14T20:05:17Z
• Authors: Estelle Nicolas; Christine Roumillac; Didier Trouche
• Keywords: Histone code; Histone Methylation; Chromatin immunoprecipitation; Heterochromatin protein 1; Dihydrofolate reductase

AbstractEpigenetic marks that specify silent heterochromatic domains in eucaryotic genomes include methylation of histone H3 lysine 9. Strikingly, active loci the vicinity are sometimes characterized by acetylation 9, suggesting balance between these two competitive modifications is important for establishment specific chromatin structures. Some euchromatic genes, targeted retinoblastoma protein Rb, also believed to be regulated 9 methylation. Here, we study dihydrofolate reductase promoter, which repressed G0 and at beginning G1 p107 or p130, Rb-related proteins. We found pocket proteins share with Rb ability associate methyl transferase SUV39H1. SUV39H1 can recruited E2F transcription factor functions as a transcriptional corepressor. With ChIP assays followed real-time PCR, showed K9 evolves from hypermethylated state hyperacetylated G1/S transition. Taken together, results indicate temporal regulation promoters may involve controlling feature previously described spatial function. ACKNOWLEDGMENTSWe thank L. Vandel, Daury, C. Monod critical reading manuscript; Chailleux O. Fayet help PCR; R. Ferreira immunoprecipitation experiments; T. Jenuwein, Sardet, Y. Nakatani materials.This work was supported grant La Ligue Nationale Contre le Cancer D.T., an équipe labellisée. E.N. studentship ARC (Association de Recherche contre Cancer).