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. 2011 Oct 3;40(3):981–995. doi: 10.1093/nar/gkr818

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© The Author(s) 2011. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 7. — The K297, K305, K307 of Repression domain and K171, K419 of P domain were acetylated by HAT of p300/CBP in vitro. (A) Schematic diagram of associated mutants. (B) Expression of associated mutants proteins in E. coli. GST-tagged proteins were immunoprecipited with GST, then ran on SDS–PAGE and stained with silver. (C) The K297, K305, K307 of Repression domain and K171, K419 of P domain are acetylated by HAT of p300/CBP in vitro. GST-tagged proteins from experiments shown in panel A were incubated with Ac-CoA and HAT in 30°C for 4 h. The reaction products were separated by SDS–PAGE and immunoblotted with the acetyl-lysine antibody. GST was as loading control.