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. 2015 Jan 27;9(12):1596–1603. doi: 10.4161/15592294.2014.983381

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© 2014 The Author(s). Published with license by Taylor & Francis Group, LLC

© Sophie T Williams, Louise J Walport, Richard J Hopkinson, Sarah K Madden, Rasheduzzaman Chowdhury, Christopher J Schofield, and Akane Kawamura

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.

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Figure 3. — KDM4A catalyzes demethylation of histone fragment peptides methylated at H3K27. MALDI-TOF spectra of KDM4A (1–359) catalyzed demethylation of (A) H3K27me3 peptide (Biotin-Ahx(aminohexanoic acid)-KAPRKQLATKAARKme3SAPATGG), (B) H3K9me3 peptide (Biotin-Ahx-ARTKQTARKme3STGGKAPRKQLA). MALDI-TOF spectra of full-length KDM4A (1–1064) catalyzed demethylation of (C) H3K27me3 peptide (KAPRKQLATKAARKme3SAPATGG) and (D) H3K9me3 peptide (Biotin-Ahx-ARTKQTARKme3STGGKAPRKQLA). FLAG-tagged full-length KDM4A (1–1064) was produced in HEK293T cells and purified from cell lysates using anti-FLAG beads prior to reaction with the histone peptide. MALDI-TOF spectra of reactions with (standard conditions, black) and without added enzyme (red) for (A)–(D) are shown. (E) Kinetic parameters determined for KDM4A (1–359) catalyzed demethylation of N^ε-trimethylated H3K9, H3K27 and H3K36 fragment peptides using FDH assay (Figure S16).