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. 2021 Jul 13;23(12):2309–2315. doi: 10.1038/s41436-021-01266-y

Fig. 1. Three pathogenic variants of PRDM9 identified in premature ovarian insufficiency (POI) patients affected its methyltransferase activity.

Fig. 1

(a) Chromatograms of the three heterozygous variants. (b) The mutant amino acids were highly conserved in mammals. (c) PRDM9 c.229C>T (p.Arg77*) localized in the KRAB domain, before the nuclear localization signal (NLS) sequence; both PRDM9 c.638T>G (p.Ile213Ser) and PRDM9 c.677A>T (p.Lys226Met) localized on PR/SET domain (residues 195–415), which determined the methyltransferase activity of PRDM9. (d) HEK293 cells were transiently transfected with wild-type (WT) or mutant PRDM9 expression vectors, the subcellular location of PRDM9 protein were indicated by FLAG (green). Scale bar: 20 μm. (e) H3K4me3 was detected by western blot in HEK293 cells overexpressing empty vector (EV), wild-type (WT) or mutant PRDM9-FLAG. (f) The relative grayscale of H3K4me3 was calculated with the use of ImageJ, and compared between subgroups.