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. 2011 Dec 15;11:178. doi: 10.1186/1471-2229-11-178

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Copyright ©2011 Wu et al; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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GmPHD5 interacted with histone H3 and recognized methylated H3K4. GST-PHD5 fusion proteins (see detail residues information in the text) were expressed in E. coli and purified (A). SDS-PAGE gel showed that histone H3 was pulled down by the GmPHD5 in the GST pull down assay (B). Western blotting showed that methylated H3K4 was present in the histone H3 pulled down by GmPHD5 (C). Peptide pull down assay indicated that GmPHD5 recognized methylated histone H3K4 with the preference to H3K4me2 (D).