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

Albig, Christian; Wang, Chao; Dann, Geoffrey P.; Wojcik, Felix; Schauer, Tamás; Krause, Silke; Maenner, Sylvain; Cai, Weili; Li, Yeran; Girton, Jack; Muir, Tom W.; Johansen, Jørgen; Becker, Peter B.; Regnard, Catherine

doi:10.1038/s41467-019-13174-6

Cited by 22 publications

(50 citation statements)

References 95 publications

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“…We used these libraries to determine the effects of histone mutations on the fundamental chromatin remodeling processes of dimer exchange and nucleosome sliding, however, the utility of these resources extends beyond the assays presented herein. Barcoded nucleosome libraries have been used to profile a variety of chromatin processes, including histone acetylation, ADP-ribosylation, phosphorylation, ubiquitylation, effector binding, and ISWI remodeling 23 , 24 , 43 – 45 . Similarly, the humanized yeast library can, in principle, be used to determine mutation-associated phenotypes beyond growth inhibition, including chromosomal instability, cell cycle inhibitor sensitivity, and DNA damage sensitivity.…”

Section: Discussionmentioning

confidence: 99%

Oncohistone mutations enhance chromatin remodeling and alter cell fates

et al. 2021

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Whole genome sequencing data mining efforts have revealed numerous histone mutations in a wide range of cancer types. These occur in all four core histones in both the tail and globular domains and remain largely uncharacterized. Here we used two high-throughput approaches, a DNA-barcoded mononucleosome library and a humanized yeast library, to profile the biochemical and cellular effects of these mutations. We identified cancer-associated mutations in the histone globular domains that enhance fundamental chromatin remodeling processes, histone exchange and nucleosome sliding, and are lethal in yeast. In mammalian cells, these mutations upregulate cancer-associated gene pathways and inhibit cellular differentiation by altering expression of lineage-specific transcription factors. This work represents a comprehensive functional analysis of the histone mutational landscape in human cancers and leads to a model in which histone mutations that perturb nucleosome remodeling may contribute to disease development and/or progression.

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Section: Discussionmentioning

confidence: 99%

Oncohistone mutations enhance chromatin remodeling and alter cell fates

et al. 2021

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“…H3S10ph also takes place in interphase, where it has been associated with transcription activation [29][30][31]. It is mediated by several kinases in mammals [32] but mostly by JIL-1 kinase in Drosophila [33][34][35]. H3S10ph allosterically inhibits the action of methyltransferases like G9A and Su(var)3-9 thus affecting HP1α recruitment [36].…”

Section: Hp1 Family Structure and Functionmentioning

confidence: 99%

How HP1 Post-Translational Modifications Regulate Heterochromatin Formation and Maintenance

Gil

Vagnarelli

2020

Cells

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Heterochromatin Protein 1 (HP1) is a highly conserved protein that has been used as a classic marker for heterochromatin. HP1 binds to di- and tri-methylated histone H3K9 and regulates heterochromatin formation, functions and structure. Besides the well-established phosphorylation of histone H3 Ser10 that has been shown to modulate HP1 binding to chromatin, several studies have recently highlighted the importance of HP1 post-translational modifications and additional epigenetic features for the modulation of HP1-chromatin binding ability and heterochromatin formation. In this review, we summarize the recent literature of HP1 post-translational modifications that have contributed to understand how heterochromatin is formed, regulated and maintained.

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“…A number of PWWP domain-containing proteins have been identified in recent years. They are associated with a variety of protein (complexes) and involved in a diverse set of functions, such as DNA repair ( 29 , 45 ), transcriptional activation ( 46 , 47 ) and repression ( 3 , 27 , 48 ), DNA methyltransferases ( 12 , 49–51 ), histone lysine methyltransferases ( 52 ) and acetyltransferases ( 53–57 ) as well as limiting the spreading of heterochromatin ( 58 , 59 ). Many of these PWWP domains preferentially bind methylated histones, with particular emphasis on methylated H3K36 or H4K20 ( 3 , 15 , 48 ).…”

Section: Discussionmentioning

confidence: 99%

H3K36 methylation and DNA-binding both promote Ioc4 recruitment and Isw1b remodeler function

Bergmann²,

Almeida³

et al. 2022

Nucleic Acids Research

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The Isw1b chromatin-remodeling complex is specifically recruited to gene bodies to help retain pre-existing histones during transcription by RNA polymerase II. Recruitment is dependent on H3K36 methylation and the Isw1b subunit Ioc4, which contains an N-terminal PWWP domain. Here, we present the crystal structure of the Ioc4-PWWP domain, including a detailed functional characterization of the domain on its own as well as in the context of full-length Ioc4 and the Isw1b remodeler. The Ioc4-PWWP domain preferentially binds H3K36me3-containing nucleosomes. Its ability to bind DNA is required for nucleosome binding. It is also furthered by the unique insertion motif present in Ioc4-PWWP. The ability to bind H3K36me3 and DNA promotes the interaction of full-length Ioc4 with nucleosomes in vitro and they are necessary for its recruitment to gene bodies in vivo. Furthermore, a fully functional Ioc4-PWWP domain promotes efficient remodeling by Isw1b and the maintenance of ordered chromatin in vivo, thereby preventing the production of non-coding RNAs.

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

Cited by 22 publications

References 95 publications

Oncohistone mutations enhance chromatin remodeling and alter cell fates

Oncohistone mutations enhance chromatin remodeling and alter cell fates

How HP1 Post-Translational Modifications Regulate Heterochromatin Formation and Maintenance

H3K36 methylation and DNA-binding both promote Ioc4 recruitment and Isw1b remodeler function

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