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. 2014 Oct 22;7:27. doi: 10.1186/1756-8935-7-27

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Copyright © 2014 Bittencourt 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 credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Mutations in the histone H3 binding surface of the G9a ankyrin repeat (ANK) domain do not abrogate binding to DNMT3A. COS- 7 cells were transiently transfected with pcDNA3.1-mDNMT3A (A and B) or pSG5-HA-mGLP full-length (D) and pSG5-FLAG-mG9a full-length (A, B and D) or pSG5-HA-mG9a.ΔANK (B). G9a was either wild-type (WT) or contained the indicated point mutations in the ANK domain. G9a, GLP and DNMT3A were immunoprecipitated from cell extracts with an anti-FLAG/anti-HA, anti-HA or anti-DNMT3A antibody, respectively. Non-immune IgG antibody was used for immunoprecipitation background estimation. Bound proteins were analyzed by immunoblot (IB) with the indicated antibodies. A 1% input sample was loaded for comparison. High (3 minutes) and low (1 minute) exposure times are shown (B). (C) Immunoblots were used to determine H3K9me2 and H3 protein levels in acid histone extracts from the indicated undifferentiated mESC lines.