title: Ectopic histone H3S10 phosphorylation causes chromatin structure remodeling in Drosophila.
abstract: Histones are subject to numerous post-translational modifications that correlate with the state of higher-order chromatin structure and gene expression. However, it is not clear whether changes in these epigenetic marks are causative regulatory factors in chromatin structure changes or whether they play a mainly reinforcing or maintenance role. In Drosophila phosphorylation of histone H3S10 in euchromatic chromatin regions by the JIL-1 tandem kinase has been implicated in counteracting heterochromatization and gene silencing. Here we show, using a LacI-tethering system, that JIL-1 mediated ectopic histone H3S10 phosphorylation is sufficient to induce a change in higher-order chromatin structure from a condensed heterochromatin-like state to a more open euchromatic state. This effect was absent when a ;kinase dead' LacI-JIL-1 construct without histone H3S10 phosphorylation activity was expressed. Instead, the 'kinase dead' construct had a dominant-negative effect, leading to a disruption of chromatin structure that was associated with a global repression of histone H3S10 phosphorylation levels. These findings provide direct evidence that the epigenetic histone tail modification of H3S10 phosphorylation at interphase can function as a causative regulator of higher-order chromatin structure in Drosophila in vivo.
authors.affiliation: Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, IA 50011, USA.
authors.forename: Huai
authors.initials: H
authors.lastname: Deng
authors.forename: Xiaomin
authors.initials: X
authors.lastname: Bao
authors.forename: Weili
authors.initials: W
authors.lastname: Cai
authors.forename: Melissa J
authors.initials: MJ
authors.lastname: Blacketer
authors.forename: Andrew S
authors.initials: AS
authors.lastname: Belmont
authors.forename: Jack
authors.initials: J
authors.lastname: Girton
authors.forename: Jørgen
authors.initials: J
authors.lastname: Johansen
authors.forename: Kristen M
authors.initials: KM
authors.lastname: Johansen
mesh_terms: D000107:Acetylation; D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism; D042002:Chromatin Assembly and Disassembly; D029721:Drosophila Proteins / Q000235:genetics / Q000378:metabolism; D004331:Drosophila melanogaster / Q000235:genetics* / Q000254:growth & development / Q000378:metabolism*; D005799:Genes, Dominant; D006579:Heterozygote; D006657:Histones / Q000378:metabolism*; D056968:Lac Repressors; D008954:Models, Biological; D016254:Mutagenesis, Insertional; D010766:Phosphorylation; D010768:Phosphoserine / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012091:Repetitive Sequences, Nucleic Acid; D012097:Repressor Proteins / Q000378:metabolism; D014158:Transcription, Genetic; D015854:Up-Regulation / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D029721:Drosophila Proteins; D006657:Histones; D056968:Lac Repressors; D011993:Recombinant Fusion Proteins; D012097:Repressor Proteins; D010768:Phosphoserine; C507306:JIL-1 protein, Drosophila; D017346:Protein Serine-Threonine Kinases