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JASPer controls interphase H3S10 phosphorylation by chromosomal kinase JIL-1 in Drosophila

ABSTRACT: JASPer controls interphase H3S10 phosphorylation by chromosomal kinase JIL-1 in Drosophila

PROVIDER: PRJNA527788 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR8743280_1.fastq.gz	Fastqsanger.gz
	SRR8743280_2.fastq.gz	Fastqsanger.gz
	SRR8743290_1.fastq.gz	Fastqsanger.gz
	SRR8743290_2.fastq.gz	Fastqsanger.gz
	SRR8743300.fastq.gz	Fastqsanger.gz

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JASPer controls interphase histone H3S10 phosphorylation by chromosomal kinase JIL-1 in Drosophila

Project description:In Drosophila the chromosomal kinase JIL-1 is responsible for most interphase histone H3S10 phosphorylation and has been proposed to protect active chromatin from acquiring heterochromatic marks, like dimethylated histone H3K9 (H3K9me2) and HP1. Here, we show that JIL-1’s targeting to chromatin depends on a PWWP domain-containing protein JASPer (JIL-1 Anchoring and Stabilizing Protein). The JASPer-JIL-1 (JJ)-complex is the major form of the kinase in vivo and is targeted to active genes and telomeric transposons via binding of the PWWP domain of JASPer to H3K36me3 nucleosomes, where the complex modulates the transcriptional output. JIL-1 and JJ-complex depletion in cycling cells lead to small changes in H3K9me2 distribution at active genes and telomeric transposons. Finally, we identify several interactors of the endogenous JJ-complex and propose that JIL-1 not only prevents heterochromatin formation but also coordinates chromatin-based regulation in the transcribed part of the genome.

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JASPer controls interphase H3S10 phosphorylation by chromosomal kinase JIL-1 in Drosophila (RNA-seq experiments)

Project description:In flies, the chromosomal kinase JIL-1 is responsible for most interphase H3S10 phosphorylation and has been proposed to protect active chromatin from acquiring heterochromatic marks like H3K9me2 and HP1. Here, we show that JIL-1’s targeting to chromatin depends on a new PWWP domain containing protein JASPer (JIL-1 Anchoring and Stabilizing Protein). The JASPer/JIL-1 (JJ)-complex is the major form of the kinase in vivo and is targeted to active genes and telomeric transposons via binding of the PWWP domain of JASPer to H3K36me3 nucleosomes. Put in place, the complex modulates the transcriptional output. JIL-1 and JJ-complex depletion in cycling cells induce small changes in H3K9me2 distribution at active genes and telomeric transposons. Finally, we identified many new interactors of the endogenous JJ-complex and propose that JIL-1 not only prevents heterochromatinisation, but also coordinates chromatin based regulation in the transcribed part of the genome.

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JASPer controls interphase H3S10 phosphorylation by chromosomal kinase JIL-1 in Drosophila (Sonication ChIP-seq experiments)

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JASPer controls interphase H3S10 phosphorylation by chromosomal kinase JIL-1 in Drosophila (MNase ChIP-seq experiments)

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JASPer controls interphase H3S10 phosphorylation by chromosomal kinase JIL-1 in Drosophila (Spike-in ChIP-seq experiments)

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JASPer controls interphase H3S10 phosphorylation by chromosomal kinase JIL-1 in Drosophila (RNA-seq experiments)

Project description:JASPer controls interphase H3S10 phosphorylation by chromosomal kinase JIL-1 in Drosophila (RNA-seq experiments)

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JASPer controls interphase H3S10 phosphorylation by chromosomal kinase JIL-1 in Drosophila (Sonication ChIP-seq experiments)

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JASPer controls interphase histone H3S10 phosphorylation by chromosomal kinase JIL-1 in Drosophila.

Project description:In flies, the chromosomal kinase JIL-1 is responsible for most interphase histone H3S10 phosphorylation and has been proposed to protect active chromatin from acquiring heterochromatic marks, such as dimethylated histone H3K9 (H3K9me2) and HP1. Here, we show that JIL-1's targeting to chromatin depends on a PWWP domain-containing protein JASPer (JIL-1 Anchoring and Stabilizing Protein). JASPer-JIL-1 (JJ)-complex is the major form of kinase in vivo and is targeted to active genes and telomeric transposons via binding of the PWWP domain of JASPer to H3K36me3 nucleosomes, to modulate transcriptional output. JIL-1 and JJ-complex depletion in cycling cells lead to small changes in H3K9me2 distribution at active genes and telomeric transposons. Finally, we identify interactors of the endogenous JJ-complex and propose that JIL-1 not only prevents heterochromatin formation but also coordinates chromatin-based regulation in the transcribed part of the genome.

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