title: Turnover of histone acetyl groups during sea urchin early development is not required for histone, heat shock and actin gene transcription.
abstract: Histone acetylation is an extremely complex, reversible and specific process. In order to evaluate the importance of this modification for gene expression during sea urchin development, acetyl group turnover of histone lysine residues was blocked by sodium butyrate. The continuous presence of 15 Mm sodium butyrate in the incubation medium from the onset of development blocked gastrulation and resulted in chromatin containing hyperacetylated histone molecules in amounts usually not found in nature. At the mesenchyme blastula stage, the expression of the early histone genes was shut off and the expression of the late genes was switched on both in control and sodium butyrate-treated embryos. Investigation of the early histone gene chromatin structure in butyrate-treated embryos revealed a random distribution of nucleosomes when the genes were transcriptionally active as compared to regular nucleosomal packaging when genes were inactive. These changes in chromatin structure during development mimicked the chromatin structural transition of the early histone genes in control embryos. In addition, the ability of heat shock genes to be induced at elevated temperature and repressed at normal temperature was unaffected in butyrate treatment of embryos. Finally, the developmental profiles of the cytoskeletal CyIIIa actin gene expression in control and butyrate-treated embryos were very similar. The data presented suggest that turnover of histone acetyl groups and the overall level of histone acetylation are not determining factors in the up and down regulation of a number of genes during early development of sea urchin.
authors.affiliation: Department of Developmental Biology, Institute of Biochemistry, Vilnius, Lithuania.
authors.forename: A
authors.initials: A
authors.lastname: Jasinskas
authors.forename: D
authors.initials: D
authors.lastname: Kersulyte
authors.forename: J
authors.initials: J
authors.lastname: Langmore
authors.forename: D
authors.initials: D
authors.lastname: Steponaviciute
authors.forename: N
authors.initials: N
authors.lastname: Jasinskiene
authors.forename: A
authors.initials: A
authors.lastname: Gineitis
mesh_terms: D000107:Acetylation; D000199:Actins / Q000096:biosynthesis; D000818:Animals; D002087:Butyrates / Q000494:pharmacology; D020148:Butyric Acid; D002843:Chromatin / Q000648:ultrastructure; D004625:Embryo, Nonmammalian / Q000187:drug effects; D047108:Embryonic Development; D004791:Enzyme Inhibitors / Q000494:pharmacology; D018507:Gene Expression Regulation, Developmental; D006360:Heat-Shock Proteins / Q000096:biosynthesis; D056572:Histone Deacetylase Inhibitors; D006657:Histones / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D008239:Lysine / Q000031:analogs & derivatives* / Q000378:metabolism; D012617:Sea Urchins; D014158:Transcription, Genetic
chemical_list: D000199:Actins; D002087:Butyrates; D002843:Chromatin; D004791:Enzyme Inhibitors; D006360:Heat-Shock Proteins; D056572:Histone Deacetylase Inhibitors; D006657:Histones; D020148:Butyric Acid; C016949:N-epsilon-acetyllysine; D008239:Lysine