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Ibf1 and Ibf2 are DNA-binding proteins required for insulator function in Drosophila

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Drosophila melanogaster

PROVIDER: GSE47559 | GEO | 2014/04/18

SECONDARY ACCESSION(S): PRJNA206064

REPOSITORIES: GEO

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Ibf1 and Ibf2 are DNA-binding proteins required for insulator function in Drosophila

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Ibf1 and Ibf2 are DNA-binding proteins required for insulator function in Drosophila [ChIP-seq]

Project description:Here we report on the identification of two previously uncharacterized proteins as CP190 interacting proteins, that we have named Ibf1 and Ibf2. These proteins localize at insulator bodies and associate with chromatin at CP190-binding sites throughout the genome. We also show that Ibf1 and Ibf2 are DNAbinding proteins that form obligated hetero-oligomers that mediate CP190 binding to chromatin. Moreover, Ibf1 and Ibf2 are necessary for insulator activity in enhancerblocking assays. Taken together our data reveal a novel pathway of CP190 recruitment to chromatin that is required for insulator activity. ChIP-Seq peak calling of CP190, Ibf1 and Ibf2 against Input sample in Drosophila melanogaster S2 cells

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Ibf1 and Ibf2 are DNA-binding proteins required for insulator function in Drosophila [ChIP-seq]

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The SNF2 and RING domain proteins FRG1 and 2 are required for RNA-directed DNA methylation in Arabidopsis

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DNA topoisomerase II modulates insulator function in Drosophila.

Project description:Insulators are DNA sequences thought to be important for the establishment and maintenance of cell-type specific nuclear architecture. In Drosophila there are several classes of insulators that appear to have unique roles in gene expression. The mechanisms involved in determining and regulating the specific roles of these insulator classes are not understood. Here we report that DNA Topoisomerase II modulates the activity of the Su(Hw) insulator. Downregulation of Topo II by RNAi or mutations in the Top2 gene result in disruption of Su(Hw) insulator function. This effect is mediated by the Mod(mdg4)2.2 protein, which is a unique component of the Su(Hw) insulator complex. Co-immunoprecipitation and yeast two-hybrid experiments show that Topo II and Mod(mdg4)2.2 proteins directly interact. In addition, mutations in Top2 cause a slight decrease of Mod(mdg4)2.2 transcript but have a dramatic effect on Mod(mdg4)2.2 protein levels. In the presence of proteasome inhibitors, normal levels of Mod(mdg4)2.2 protein and its binding to polytene chromosomes are restored. Thus, Topo II is required to prevent Mod(mdg4)2.2 degradation and, consequently, to stabilize Su(Hw) insulator-mediated chromatin organization.

| S-EPMC3029388 | biostudies-literature

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