Figure 2

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Unrepaired DNA breaks suppress NHK-1 kinase activity.

(A) H2A T119 phosphorylation in wild type, nhk-1E24/Df and spnD2. Ovaries at stage 5–7 were immunostained with anti-dH2ApT119 antibody and propidium iodide. Arrowheads indicate meiotic chromosomes in oocytes. Bar = 10 µm. (B) The H2ApT119 signal intensity on the chromosomes in oocytes was measured relative to that in follicle cells. The bars on the graph represent standard error of the mean (SEM). A minimum of eight oocytes from each genotype were quantified. NHK-1 activity measured by H2A T119 phosphorylation was significantly reduced in nhk-1 and spn mutant oocytes (p<0.01; marked with asterisks). H2A T119 phosphorylation in oocytes expressing wild-type BAF and non-phosphorylatable BAF (BAF-3A) was comparable to that in wild type, indicating the karyosome abnormality itself is not the cause of low dH2ApT119 signals in spn mutants.

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