title: Histone acetylation is involved in hsp70 gene transcription regulation in Drosophila melanogaster.
abstract: The acetylation/deacetylation modifications of N-terminal tails of core histones play critical roles in activation/repression of many eukaryotic genes. However, the role of acetylation in transcription regulation of heat shock protein genes (hsp) is still a disputed issue. In this study, we investigated the influences of histone acetylation modification on changes in structure of polytene chromosomes and in expression of hsp70 gene in Drosophila melanogaster, by using histone deacetylase (HDAC) inhibitors Trichostatin A (TSA) and sodium butyrate (BuA), and the heat shock treatment of larvae of the flies. The results presented in this paper demonstrate that both TSA and BuA were able to affect the chromatin structure at the site where hsp70 gene is located along the polytene chromosome. Furthermore, the HDAC inhibitors significantly promoted the hsp70 gene transcription, at an extent similar to that induced by heat shock. The immunofluorescence in situ localization study further confirmed that the hsp70 gene locus was hyperacetylated after the heat induction. We therefore conclude that histone acetylation can significantly enhance both the basal and the inducible expression of hsp70 gene in D. melanogaster and hence plays important roles in hsp gene regulation. This study has provided a basis and a framework for further investigations aimed at the establishment of the correlation between acetylation modification and hsp gene regulation.
authors.affiliation: Institute of Genetics and Cytology, Northeast Normal University, Changchun, China.
authors.forename: Ting
authors.initials: T
authors.lastname: Chen
authors.forename: Hui
authors.initials: H
authors.lastname: Sun
authors.forename: Jun
authors.initials: J
authors.lastname: Lu
authors.forename: Yanmei
authors.initials: Y
authors.lastname: Zhao
authors.forename: Dan
authors.initials: D
authors.lastname: Tao
authors.forename: Xiaoxue
authors.initials: X
authors.lastname: Li
authors.forename: Baiqu
authors.initials: B
authors.lastname: Huang
mesh_terms: D000107:Acetylation; D000818:Animals; D002087:Butyrates / Q000494:pharmacology; D002875:Chromosomes / Q000187:drug effects; D029721:Drosophila Proteins / Q000235:genetics* / Q000378:metabolism; D004331:Drosophila melanogaster / Q000235:genetics*; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005455:Fluorescent Antibody Technique; D005786:Gene Expression Regulation; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics* / Q000378:metabolism; D056572:Histone Deacetylase Inhibitors; D006657:Histones / Q000378:metabolism*; D006877:Hydroxamic Acids / Q000494:pharmacology; D007814:Larva; D012469:Salivary Glands / Q000187:drug effects / Q000502:physiology; D014158:Transcription, Genetic
chemical_list: D002087:Butyrates; D029721:Drosophila Proteins; D004791:Enzyme Inhibitors; D018840:HSP70 Heat-Shock Proteins; D056572:Histone Deacetylase Inhibitors; D006657:Histones; D006877:Hydroxamic Acids; C012589:trichostatin A