Figure S1 (related to Figure 1). Effects of Kdm2a, KDM2A, or KDM2B on the putative histone H3 substrates and evaluation of KDM2A and KDM2B siRNAs. (A) Kdm2a overexpression did not change the general levels of methylated H3 at lys36. H3: loading control. (B) RT-PCR detection of the efficiency of KDM2A siRNAs on blocking KDM2A and β-Catenin transcripts. GAPDH: loading control. RT-: samples without reverse transcriptase. (C) Luciferase assays showing the effect of KDM2A inhibition via siRNA on the activity of the Wnt-responsive reporter. Error bars show the SEM of four replicates. *p<0.05; **p<0.01; ns: not significant. (D) Rescue of KDM2A knockdown by cotransfection of Xenopus Kdm2a plasmid. (E) Knockdown of KDM2A did not affect the general levels of methylated H3 at lys36. H3: loading control. (F) RT-PCR detection of the efficiency of KDM2B siRNAs on blocking KDM2A transcript. GAPDH: loading control. RT-: samples without reverse transcriptase. (G) KDM2B knockdown upregulated β-Catenin. Actin: loading control. (H) KDM2B knockdown caused no significant influence on the general level of its putative histone substrate. H3: loading control. (I) Simultaneous knockdown of KDM2A and 2B led to a synergistic effect on reporter activity. Cellular histone extracts were used for IB in (A), (E) and (H), and WCL were used for IB in (D) and (G).
Image published in: Lu L et al. (2015)
Copyright © 2015. Image reproduced with permission of the Publisher, Elsevier B. V.
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