H3S10 phosphorylation by the JIL-1 kinase regulates H3K9 dimethylation and gene expression at the white locus in Drosophila

Wang, Chao; Cai, Weili; Li, Yeran; Girton, Jack; Johansen, Jørgen; Johansen, Kristen M.

doi:10.4161/fly.20029

Cited by 13 publications

(29 citation statements)

References 20 publications

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“…Interestingly, although the CTD of JIL-1 binds to the NH 2 -terminal tail of histone H3, modeling of the three-dimensional structure of JIL-1 relative to nucleosome structure suggested that JIL-1 is likely to phosphorylate H3 of one or more nucleosomes some distance away from this binding site. 5 Taken together, these findings suggest a model where the NTD of JIL-1 is required for chromatin complex interactions that position the kinase domain(s) for catalytic activity in the context of the state of higher order nucleosome packaging and chromatin structure, whereas sequences in the CTD mediate binding to specific chromatin sites. Furthermore, it has been demonstrated that sequences within both the NTD and CTD are required for enrichment of JIL-1 on the male X chromosome (12).…”

Section: Discussionmentioning

confidence: 78%

“…In Drosophila, histone H3 serine 10 (H3S10) 4 phosphorylation by the JIL-1 kinase at interphase functions to maintain active gene expression by serving as a protective epigenetic mark counteracting spreading of H3K9 dimethylation and gene silencing (1)(2)(3)(4)(5). Furthermore, JIL-1 is enriched about 2-fold on the male X chromosome and implicated in dosage compensation of transcription due to its association with the male-specific lethal complex (6 -9).…”

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confidence: 99%

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Domain Requirements of the JIL-1 Tandem Kinase for Histone H3 Serine 10 Phosphorylation and Chromatin Remodeling in Vivo

Cai

Wang

et al. 2013

Journal of Biological Chemistry

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Background:The JIL-1 histone H3 serine 10 (H3S10) tandem kinase functions to maintain active gene expression. Results:The NH 2 -terminal domain and both kinase domains are required for H3S10 kinase activity. Conclusion:The NH 2 -terminal domain is required for chromatin complex interactions, and H3S10 phosphorylation functions as a causative regulator of chromatin structure. Significance: Determining how the domain structure of JIL-1 contributes to its function is crucial for understanding regulation of gene expression.

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Section: Discussionmentioning

confidence: 78%

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confidence: 99%

Domain Requirements of the JIL-1 Tandem Kinase for Histone H3 Serine 10 Phosphorylation and Chromatin Remodeling in Vivo

Cai

Wang

et al. 2013

Journal of Biological Chemistry

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“…that showed association of H3K9me2 spreading with decreased gene expression (27)(28)(29)(30). To examine this on a genome-wide scale, we stratified all of the genes into those in H3K9me2-spreading domains (3,930) and genes that are not in H3K9me2 in either control or Ni-exposed cells (8,096) ( Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Ni-induced spreading of H3K9me2 is reminiscent of the local discrete changes, suggesting that misregulation of this regulatory switch results in altered gene expression. Furthermore, several earlier studies have suggested ectopic spreading of H3K9me2 to be an important signal for transcriptional silencing (27)(28)(29)(30)39). However, the alternate possibility of gene silencing resulting in spreading of H3K9me2 in a subset of the spreading domains cannot be ruled out.…”

Section: Discussionmentioning

confidence: 95%

Epigenetic dysregulation by nickel through repressive chromatin domain disruption

Jose

Jagannathan

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Investigations into the genomic landscape of histone modifications in heterochromatic regions have revealed histone H3 lysine 9 dimethylation (H3K9me2) to be important for differentiation and maintaining cell identity. H3K9me2 is associated with gene silencing and is organized into large repressive domains that exist in close proximity to active genes, indicating the importance of maintenance of proper domain structure. Here we show that nickel, a nonmutagenic environmental carcinogen, disrupted H3K9me2 domains, resulting in the spreading of H3K9me2 into active regions, which was associated with gene silencing. We found weak CCCTC-binding factor (CTCF)-binding sites and reduced CTCF binding at the Ni-disrupted H3K9me2 domain boundaries, suggesting a loss of CTCF-mediated insulation function as a potential reason for domain disruption and spreading. We furthermore show that euchromatin islands, local regions of active chromatin within large H3K9me2 domains, can protect genes from H3K9me2-spreadingassociated gene silencing. These results have major implications in understanding H3K9me2 dynamics and the consequences of chromatin domain disruption during pathogenesis.insulator | nickel toxicity | nickel carcinogenesis

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“…To further validate these findings, we performed ChIP assays as in Wang et al. (6,9) for five randomly selected genes among the genes analyzed above. Chromatin was immunoprecipitated (ip) from wild-type or JIL-1 null mutant larval salivary glands using rabbit anti-H3S10ph antibody or purified rabbit IgG antibody (negative control) or mAbs to H3K9me2 or GST (negative control).…”

Section: Resultsmentioning

confidence: 99%

Genome-wide analysis of regulation of gene expression and H3K9me2 distribution by JIL-1 kinase mediated histone H3S10 phosphorylation in Drosophila

Cai

Wang

et al. 2014

Nucleic Acids Research

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In this study we have determined the genome-wide relationship of JIL-1 kinase mediated H3S10 phosphorylation with gene expression and the distribution of the epigenetic H3K9me2 mark. We show in wild-type salivary gland cells that the H3S10ph mark is predominantly enriched at active genes whereas the H3K9me2 mark is largely associated with inactive genes. Comparison of global transcription profiles in salivary glands from wild-type and JIL-1 null mutant larvae revealed that the expression levels of 1539 genes changed at least 2-fold in the mutant and that a substantial number (49%) of these genes were upregulated whereas 51% were downregulated. Furthermore, the results showed that downregulation of genes in the mutant was correlated with higher levels or acquisition of the H3K9me2 mark whereas upregulation of a gene was correlated with loss of or diminished H3K9 dimethylation. These results are compatible with a model where gene expression levels are modulated by the levels of the H3K9me2 mark independent of the state of the H3S10ph mark, which is not required for either transcription or gene activation to occur. Rather, H3S10 phosphorylation functions to indirectly maintain active transcription by counteracting H3K9 dimethylation and gene silencing.

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H3S10 phosphorylation by the JIL-1 kinase regulates H3K9 dimethylation and gene expression at the white locus in Drosophila

Cited by 13 publications

References 20 publications

Domain Requirements of the JIL-1 Tandem Kinase for Histone H3 Serine 10 Phosphorylation and Chromatin Remodeling in Vivo

Domain Requirements of the JIL-1 Tandem Kinase for Histone H3 Serine 10 Phosphorylation and Chromatin Remodeling in Vivo

Epigenetic dysregulation by nickel through repressive chromatin domain disruption

Genome-wide analysis of regulation of gene expression and H3K9me2 distribution by JIL-1 kinase mediated histone H3S10 phosphorylation in Drosophila

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