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. 2008 Feb 7;36(5):1690–1702. doi: 10.1093/nar/gkn009

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© 2008 The Author(s)

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) 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. — Analysis of the affinity and specificity of the binding of Glis3 and Gli1 to Glis-BS. (A) Binding of Glis3 to Glis-BS. The binding of His₆-Glis3(ZFD) to radiolabeled Glis-BS was examined by EMSA as a function of increasing concentrations of Glis-BS as indicated (top panel). The amount of bound and free Glis-BS was determined and the K_d calculated by Scatchard plot analysis (lower panel). (B) Binding of Gli1 to Glis-BS. The binding of His₆-Gli1(ZFD) to radiolabeled Glis-BS was examined by EMSA as a function of increasing concentrations of Glis-BS as indicated (top panel). The amount of bound and free Glis-BS was determined and the K_d calculated by Scatchard plot analysis (lower panel). (C) Effect of various mutations in Glis-BS on Glis3 binding. EMSA analysis was performed with His₆-Glis3(ZFD) and the ³²P-labeled consensus Glis-BS (0.5 nM) in the absence and presence of 5- or 25-fold excess of unlabeled Glis-BS or mutant Glis-BS (M1-M14) as indicated. The sequences of the M1-M14 mutants are shown beneath the EMSA. The mutated nucleotides are underlined.