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

TitleJASPer controls interphase histone H3S10 phosphorylation by chromosomal kinase JIL-1 in Drosophila.
Publication TypeJournal Article
Year of Publication2019
AuthorsAlbig, C, Wang, C, Dann, GP, Wojcik, F, Schauer, T, Krause, S, Maenner, S, Cai, W, Li, Y, Girton, J, Muir, TW, Johansen, J, Johansen, KM, Becker, PB, Regnard, C
JournalNat Commun
Volume10
Issue1
Pagination5343
Date Published2019 11 25
ISSN2041-1723
KeywordsAnimals, Cell Line, Chromatin, Chromatin Assembly and Disassembly, Drosophila melanogaster, Drosophila Proteins, Heterochromatin, Histones, Humans, Interphase, Methylation, Phosphorylation, Protein Processing, Post-Translational, Protein-Serine-Threonine Kinases
Abstract

<p>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.</p>

DOI10.1038/s41467-019-13174-6
Alternate JournalNat Commun
PubMed ID31767855
PubMed Central IDPMC6877644
Grant ListR01 GM062916 / GM / NIGMS NIH HHS / United States
R01 GM107047 / GM / NIGMS NIH HHS / United States
R37 GM086868 / GM / NIGMS NIH HHS / United States