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. 2011 Jul 14;6(7):e22290. doi: 10.1371/journal.pone.0022290

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Foreman et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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(A) SMYD3 trimethylates H4-K20. Right panel: unmethylated [H4(0)], mono-[H4(1)], di-[H4(2)], and, as a negative control, tri-methylated [H4(3)] peptides were employed in an in vitro HMTase proximity bead assay with baculoviral SMYD3 and SMYD1 (negative control). Degree of methylation was measured by scintillation counting in CPM. Left panels: Western analysis using anti-mono- and trimethyl-specific antibodies (Upstate) confirm in vitro specificity of SMYD3 for H4-K20me3. (B) SMYD3 preferentially trimethylates H4-K20 in reconstituted chromatin. Recombinant oocyte nucelosomes were assembled into chromatin, followed by in vitro HMTase assays and SDS-PAGE resolution of reaction products. SMYD3 inputs were increased from 0.5 µg to 2.4 µg, (triangle above lanes), and western analyses were performed with the indicated histone H4 methylation state-specific antibodies (middle panels), with a pan-anti-H4 (lower panel) providing a loading control for chromatin input.