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. 2009 Aug 10;186(3):355–362. doi: 10.1083/jcb.200905153

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© 2009 Mérino et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 1. — BH3 replacements in Bim alter its binding profile. (A) Interactions between Bcl-2 family members show the rationale of our experiments. Bad binds Bcl-2, Bcl-x_L, and Bcl-w, whereas Noxa binds only Mcl-1 and A1. Bim and Puma bind all of their prosurvival relatives, but Bim (the Bim_S isoform) binds Bax, whereas Puma does not. (B) Amino acids 140–161 of mouse Bim_EL (red) were replaced by the BH3 sequences of mouse Bad, NoxaA, or Puma. Boxed sequences indicate the 26-mer peptides used to measure the affinities of the mutant BH3 peptides for mouse Bcl-x_L, Mcl-1, and Bax. (C) Nanomolar affinities of the BH3 peptides for GST–Bcl-x_L and GST–Mcl-1 as measured on an S51 biosensor. (D) Tests for binding of the same peptides to Bax. The dashed line corresponds to the method used to determine the IC50 value. Starting from the left side, 50% binding of Bim to Bax occurs when a concentration of 3.1 µM of peptide is present in the system. The horizontal dashed line is for the 50%, the place where it intersects with the curve determines the position of the vertical line, and the reading is made on the peptide concentration scale.