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A model has been proposed in which JIL-1 kinase-mediated H3S10 and H2Av phosphorylation is required for transcriptional elongation and heat shock-induced chromatin decondensation. However, here we show that although H3S10 phosphorylation is indeed compromised in the H2Av null mutant, chromatin decondensation at heat shock loci is unaffected in the absence of JIL-1 as well as of H2Av and that there is no discernable decrease in the elongating form of RNA polymerase II in either mutant. Furthermore, mRNA for the major heat shock protein Hsp70 is transcribed at robust levels in both H2Av and JIL-1 null mutants. Using a different chromatin remodeling paradigm that is JIL-1 dependent, we provide evidence that ectopic tethering of JIL-1 and subsequent H3S10 phosphorylation recruits PARP-1 to the remodeling site independently of H2Av phosphorylation. These data strongly suggest that H2Av or H3S10 phosphorylation by JIL-1 is not required for chromatin decondensation or transcriptional elongation in Drosophila.
Pubmed ID: 28807902 RIS Download
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View all literature mentionsThis monoclonal targets Histone H3 (Dimethyl K9 Phospho S10) clone 6HH3-2C5
View all literature mentionsThis polyclonal targets Histone H3
View all literature mentionsThis polyclonal targets Green Fluorescent Protein (GFP)
View all literature mentionsThis polyclonal targets Phospho-Histone H3 (Ser10)
View all literature mentionsThis monoclonal targets histone 2A gamma variant, phosphorylated
View all literature mentionsThis monoclonal targets α-Tubulin
View all literature mentionsThis monoclonal targets RNA Polymerase II H14
View all literature mentionsThis monoclonal targets RNA Polymerase II
View all literature mentionsThis monoclonal targets Histone H3 (di methyl K9) antibody [mAbcam 1220] - ChIP Grade
View all literature mentionsThis monoclonal targets Histone H3 (phospho S10)
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