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Histone Phosphoacetylation ChIP-seq of Kc167 cells from Drosophila

ABSTRACT: ChIP-seq was performed using Drosophila Kc167 cells using antibodies against H3K4me3 to identify active promoters and H3K4me1 to identify active enhancers. H3K27ac ChIPseq was performed to identify active promoters and enhancers. Once enhancers and promoters were identified, JIL-1 and histone phosphorylation, H3K9acS10ph and H3K27acS28ph, ChIP-seq was performed to look at binding trends. JIL-1 and phosphoacetlation is found at low levels at inactive enhancers and shows increase at active enhancers and promoters. Here we examine histone phosphorylation by JIL-1 and acetylation of H3K27ac by CBP at transcriptionally active vs. inactive promoters and enhancers. ChIP-seq is performed in Kc167 Drosophila cells using antibodies against JIL-1, H3K27acS28ph, H3K9acS10ph, H3K4me3, H3K4me1, and H3K27ac.

ORGANISM(S): Drosophila melanogaster

SUBMITTER: Wendy Kellner

PROVIDER: E-GEOD-36374 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Genome-wide phosphoacetylation of histone H3 at Drosophila enhancers and promoters.

Kellner Wendy A WA Ramos Edward E Van Bortle Kevin K Takenaka Naomi N Corces Victor G VG

Genome research 20120416 6

Transcription regulation is mediated by enhancers that bind sequence-specific transcription factors, which in turn interact with the promoters of the genes they control. Here, we show that the JIL-1 kinase is present at both enhancers and promoters of ecdysone-induced Drosophila genes, where it phosphorylates the Ser10 and Ser28 residues of histone H3. JIL-1 is also required for CREB binding protein (CBP)-mediated acetylation of Lys27, a well-characterized mark of active enhancers. The presence ...[more]

PMID: 22508764

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Histone Phosphoacetylation ChIP-seq of Kc167 cells from Drosophila

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