Histone H3 lysine 4 trimethylation regulates cotranscriptional H2A variant exchange by Tip60 complexes to maximize gene expression
Copyright policy )Histone H3 lysine 4 trimethylation regulates cotranscriptional H2A variant exchange by Tip60 complexes to maximize gene expression
Significance Histone H3 trimethylated at lysine 4 and the hyperacetylated H2A variant, H2A.Z/v, are found at nucleosomes near promoters of highly expressed loci including the stress response genes. This study uses the inducible hsp70 loci from Drosophila to demonstrate that the dTip60 chromatin remodeling complex incorporates and acetylates H2A.Z/v in a transcription-dependent manner to maximize the rates of Pol II release into elongation. In vivo and in vitro evidence is provided showing that H3 lysine 4 trimethylation regulates both the H2A.Z/v exchange and histone acetyltransferase activities of Tip60 complexes to ensure that nucleosome destabilization at promoters only occurs during transcription.
- Rutgers, The State University of New Jersey United States
Lysine, Acetylation, DNA Polymerase II, Histone-Lysine N-Methyltransferase, Methylation, Models, Biological, Nucleosomes, DNA-Binding Proteins, Histones, Drosophila melanogaster, Gene Expression Regulation, Heat Shock Transcription Factors, Genetic Loci, Multiprotein Complexes, Animals, Drosophila Proteins, HSP70 Heat-Shock Proteins, Promoter Regions, Genetic, Histone Acetyltransferases, Protein Binding
Lysine, Acetylation, DNA Polymerase II, Histone-Lysine N-Methyltransferase, Methylation, Models, Biological, Nucleosomes, DNA-Binding Proteins, Histones, Drosophila melanogaster, Gene Expression Regulation, Heat Shock Transcription Factors, Genetic Loci, Multiprotein Complexes, Animals, Drosophila Proteins, HSP70 Heat-Shock Proteins, Promoter Regions, Genetic, Histone Acetyltransferases, Protein Binding
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