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. 2015 Oct 1;142(19):3416–3428. doi: 10.1242/dev.121871

Fig. 5.

Fig. 5.

Prdm12 function requires both the PR and zinc-finger domains and acts as a G9a-dependent repressor to induce en1. (A) Diagram of the Flag-mPrdm12 wild-type and mutants. (B) Average number of En1+ cells detected on the electroporated side of embryos overexpressing the indicated constructs. *, P<0.05; **, P<0.01; ***, P<0.001; n≥3. (C) Top panels: scheme of the VP16-Prdm12 and EnR-Prdm12 constructs and transverse sections of the neural tube of embryos overexpressing the indicated constructs (250 pg/blastomere for EnR-Prdm12 and 50 pg/blastomere for VP16-Prdm12) hybridized with the indicated probes. The upregulation of en1 by EnR-Prdm12, the downregulation of en1 and the upregulation of nkx6-1 by VP16-Prdm12 are indicated (arrows). Bottom panels: RT-PCR analysis of the expression of the indicated genes in RA-treated neuralized animal caps overexpressing mouse Prdm12 (250 pg/blastomere), EnR-Prdm12 (250 pg/blastomere) or VP16-Prdm12 (50 pg/blastomere) mRNA as indicated. (D) A dominant negative form of G9a (25, 500 and 100 pg mRNA injected) reduces the ability of Prdm12 to induce en1 and slightly attenuates the repression of dbx1 and nkx6-1 in RA-treated neuralized animal caps. (E) The mouse-amphioxus Prdm12 chimeric protein aPR-mZF, but not the complementary chimeric protein mPR-aZF, induces en1 and represses dbx1 and nkx6-1 in RA-treated neuralized animal caps.