Ecdysone induced gene expression is associated with acetylation of histone H3 lysine 23 in Drosophila melanogaster
Posttranslational modification of histones regulates transcription but the exact role that acetylation of specific lysine residues plays in biological processes in vivo is still not clearly understood. To assess the contribution of different histone modifications to transcriptional activation in viv...
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description | Posttranslational modification of histones regulates transcription but the exact role that acetylation of specific lysine residues plays in biological processes in vivo is still not clearly understood. To assess the contribution of different histone modifications to transcriptional activation in vivo, we determined the acetylation patterns on the ecdysone induced Eip74EF and Eip75B genes in Drosophila melanogaster larvae by chromatin immunoprecipitation. We found that acetylation of histone H3 lysine 23 is localized to promoters and correlates with endogenous ecdysone induced gene activation. In contrast, acetylation of lysines 8, 12 and 16 of histone H4 and lysine 9 of histone H3 showed minor differences in their distribution on the regulatory and transcribed regions tested, and had limited or no correlation with ecdysone induced transcriptional activity. We found that dCBP, which is encoded by the nejire gene, acetylates H3 lysine 23 in vivo, and silencing of nejire leads to reduced expression of the Eip74EF and Eip75B genes. Our results suggest that acetylation of specific lysine residues of histones contribute specifically to the dynamic regulation of transcription. Furthermore, along with previous studies identify CBP dependent H3 lysine 23 acetylation as an evolutionarily conserved chromatin modification involved in steroid induced gene activation. |
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To assess the contribution of different histone modifications to transcriptional activation in vivo, we determined the acetylation patterns on the ecdysone induced Eip74EF and Eip75B genes in Drosophila melanogaster larvae by chromatin immunoprecipitation. We found that acetylation of histone H3 lysine 23 is localized to promoters and correlates with endogenous ecdysone induced gene activation. In contrast, acetylation of lysines 8, 12 and 16 of histone H4 and lysine 9 of histone H3 showed minor differences in their distribution on the regulatory and transcribed regions tested, and had limited or no correlation with ecdysone induced transcriptional activity. We found that dCBP, which is encoded by the nejire gene, acetylates H3 lysine 23 in vivo, and silencing of nejire leads to reduced expression of the Eip74EF and Eip75B genes. Our results suggest that acetylation of specific lysine residues of histones contribute specifically to the dynamic regulation of transcription. Furthermore, along with previous studies identify CBP dependent H3 lysine 23 acetylation as an evolutionarily conserved chromatin modification involved in steroid induced gene activation.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0040565</identifier><identifier>PMID: 22808194</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Acetates ; Acetylation ; Acetylation - drug effects ; Acetyltransferases - metabolism ; Androgens ; Animals ; Apoptosis ; Biochemistry ; Biological activity ; Biology ; Breast cancer ; Chromatin ; Deoxyribonucleic acid ; DNA ; DNA binding proteins ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; Drosophila ; Drosophila melanogaster - drug effects ; Drosophila melanogaster - genetics ; Drosophila melanogaster - growth & development ; Drosophila Proteins - genetics ; Drosophila Proteins - metabolism ; Ecdysone ; Ecdysone - pharmacology ; Epigenetics ; Gene expression ; Gene Expression Regulation - drug effects ; Gene regulation ; Genes ; Genes, Insect - genetics ; Genetic aspects ; Genetics ; Genomes ; Histone H3 ; Histone H4 ; Histones ; Histones - metabolism ; Immunoprecipitation ; In vivo methods and tests ; Insects ; Larva - genetics ; Larva - growth & development ; Larvae ; Life Sciences ; Lysine ; Lysine - metabolism ; Microscopy ; Models, Genetic ; Molecular biology ; Mutation ; Ontology ; p300-CBP Transcription Factors - metabolism ; Post-translational modifications ; Promoter Regions, Genetic - genetics ; Protein Processing, Post-Translational - drug effects ; Protein Processing, Post-Translational - genetics ; Proteins ; Residues ; Thyroid gland ; Time Factors ; Transcription (Genetics) ; Transcription activation ; Transcription Factors - genetics ; Transcription Factors - metabolism ; Transcription, Genetic - drug effects</subject><ispartof>PloS one, 2012-07, Vol.7 (7), p.e40565</ispartof><rights>COPYRIGHT 2012 Public Library of Science</rights><rights>2012 Bodai et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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To assess the contribution of different histone modifications to transcriptional activation in vivo, we determined the acetylation patterns on the ecdysone induced Eip74EF and Eip75B genes in Drosophila melanogaster larvae by chromatin immunoprecipitation. We found that acetylation of histone H3 lysine 23 is localized to promoters and correlates with endogenous ecdysone induced gene activation. In contrast, acetylation of lysines 8, 12 and 16 of histone H4 and lysine 9 of histone H3 showed minor differences in their distribution on the regulatory and transcribed regions tested, and had limited or no correlation with ecdysone induced transcriptional activity. We found that dCBP, which is encoded by the nejire gene, acetylates H3 lysine 23 in vivo, and silencing of nejire leads to reduced expression of the Eip74EF and Eip75B genes. Our results suggest that acetylation of specific lysine residues of histones contribute specifically to the dynamic regulation of transcription. Furthermore, along with previous studies identify CBP dependent H3 lysine 23 acetylation as an evolutionarily conserved chromatin modification involved in steroid induced gene activation.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>22808194</pmid><doi>10.1371/journal.pone.0040565</doi><tpages>e40565</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Public Library of Science (PLoS); PubMed Central; Free Full-Text Journals in Chemistry |
subjects | Acetates Acetylation Acetylation - drug effects Acetyltransferases - metabolism Androgens Animals Apoptosis Biochemistry Biological activity Biology Breast cancer Chromatin Deoxyribonucleic acid DNA DNA binding proteins DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Drosophila Drosophila melanogaster - drug effects Drosophila melanogaster - genetics Drosophila melanogaster - growth & development Drosophila Proteins - genetics Drosophila Proteins - metabolism Ecdysone Ecdysone - pharmacology Epigenetics Gene expression Gene Expression Regulation - drug effects Gene regulation Genes Genes, Insect - genetics Genetic aspects Genetics Genomes Histone H3 Histone H4 Histones Histones - metabolism Immunoprecipitation In vivo methods and tests Insects Larva - genetics Larva - growth & development Larvae Life Sciences Lysine Lysine - metabolism Microscopy Models, Genetic Molecular biology Mutation Ontology p300-CBP Transcription Factors - metabolism Post-translational modifications Promoter Regions, Genetic - genetics Protein Processing, Post-Translational - drug effects Protein Processing, Post-Translational - genetics Proteins Residues Thyroid gland Time Factors Transcription (Genetics) Transcription activation Transcription Factors - genetics Transcription Factors - metabolism Transcription, Genetic - drug effects |
title | Ecdysone induced gene expression is associated with acetylation of histone H3 lysine 23 in Drosophila melanogaster |
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