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. 2015 Jan 20;43(3):1869–1882. doi: 10.1093/nar/gkv013

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© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 4. — Inclusion of SUV39H2 exon 3 is required to encode an active histone methyltransferase. (A) In vitro analysis of the methyltransferase activity associated to each _FVG9A and _FVSUV39H2 isoforms. Scheme of the in vitro histone methyltransferase (HMT) assay procedure (left panel). Various quantities of purified _FVG9A and _FVSUV39H2 (right panel) were incubated with the recombinant human histone H3.1 and S-adénosylméthionine (SAM) producing methylated H3.1 and S-adenosylhomocysteine (SAH). Histone H3 and H3K9me3 were analyzed by western blot using specific antibodies (right panel). Control reactions were supplemented with _FVTomato, water (-) or sample issued from blank purification procedure (Ctl). Levels of recombinant proteins were estimated using V5 antibody. (B) and (C) H3K9me3 was assessed in HeLa cells after expression of _FVG9A and _FVSUV39H2 isoforms. (B) DNA was counterstained with DAPI (blue), H3K9me3 was immunostained with a specific antibody (red) and cells expressing _FVG9A and _FVSUV39H2 were revealed with ZsGreen1 Fluorescence Protein (ZsGFP panel; labeled with white arrows in H3K9me3 panel). (C) Analysis of H3K9me3, H3K9me2 and H3 levels by western blot in total protein extracts of HeLa cells expressing _FVG9A and _FVSUV39H2 isoforms.