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. 2013 Dec 5;105(2):202–210. doi: 10.1111/cas.12322

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© 2013 The Authors. Cancer Science published by Wiley Publishing Asia Pty Ltd on behalf of Japanese Cancer Association.

This is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is noncommercial and no modifications or adaptations are made.

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Fig. 7 — A novel mutation in the RNF8 gene and the reduced ability of TE-6 cells to polyubiquitinate γ-H2AX. (a) The structure of RNF8 protein and a newly identified T448M amino acid-substitution mutation. (b) Western blot analysis of γ-H2Ax in TE-6 and TE-1 cells treated with 2 Gy of X-rays. (c) The proportion of diubiquitinated γ-H2Ax standardized to non-ubiquitinated γ-H2Ax. The data represent the averages and standard deviations of three independent experiments. (d) The proportion of monoubiquitinated γ-H2Ax standardized to non-ubiquitinated γ-H2Ax. The data represent the averages and standard deviations of three independent experiments.