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

Christian Albig, Chao Wang, Geoffrey P. Dann, Felix Wojcik, Tamás Schauer, Silke Krause, Sylvain Maenner, Weili Cai, Yeran Li, Jack Girton, Tom W. Muir, Jørgen Johansen, Kristen M. Johansen, Peter B. Becker () and Catherine Regnard ()
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Christian Albig: LMU Munich
Chao Wang: Iowa State University
Geoffrey P. Dann: Princeton University
Felix Wojcik: Princeton University
Tamás Schauer: LMU Munich
Silke Krause: LMU Munich
Sylvain Maenner: LMU Munich
Weili Cai: Iowa State University
Yeran Li: Iowa State University
Jack Girton: Iowa State University
Tom W. Muir: Princeton University
Jørgen Johansen: Iowa State University
Kristen M. Johansen: Iowa State University
Peter B. Becker: LMU Munich
Catherine Regnard: LMU Munich

Nature Communications, 2019, vol. 10, issue 1, 1-17

Abstract: Abstract 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.

Date: 2019
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DOI: 10.1038/s41467-019-13174-6

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