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. 2012 Jun 29;40(17):8285–8295. doi: 10.1093/nar/gks645

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© The Author(s) 2012. 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 1. — Overview of nucleosomes used in this study. (A) Domain organization of full-length macroH2A, and the truncations used in this study compared with major-type H2A. The truncated macroH2A construct, mH2A₁₂₂, possesses only the histone-fold portion of macroH2A, and mH2A₁₆₁ additionally contains the basic macro-linker. (B) Nucleosomes and histone oligomers analyzed by SDS PAGE. To confirm the sizes and ratios of histone proteins in reconstituted nucleosomes, nucleosomes containing major-type H2A (lane 1), mH2A₁₂₂ (lane 3) and mH2A₁₆₁ (lane 6) were run alongside the histone components: the histone octamer with major-type H2A (lane 2), mH2A₁₂₂-H2B dimer (lane 4), (H3-H4)₂ tetramer (lane 5) and mH2A₁₆₁-H2B dimer (lane 7). (C) Nucleosomes analyzed by native PAGE. Fluorescently labeled nucleosomes (centered 30-N-33 and end-positioned 0-N-33) were produced with either major-type H2A, mH2A₁₂₂ or mH2A₁₆₁ as indicated.