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. 2012 Jan 10;40(9):3898–3912. doi: 10.1093/nar/gkr1296

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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 5. — T98 is not a phosphorylation site and the T98A mutation disturbs the folding and pT-binding of the FHA domain. (A) Phosphorylation of MDC1 FHA proteins by HeLa cell nuclear extracts (NE) in the presence of ³²P-γ-ATP. (B) SMT3-MDC1^2–133 and its T98A mutant were eluted in a Superdex 200 10/300 GL column and in buffer 20 mM sodium phosphate (pH 7.6) and 250 mM NaCl. SDS-PAGE gels of the fractions are shown at the bottom. (C) ITC analysis of SMT3-MDC1^2–133 and its T98A mutant with phosphopeptide pT4-8P in 20 mM sodium phosphate (pH 7.6) and 250 mM NaCl.