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. Author manuscript; available in PMC: 2010 Mar 28.
Published in final edited form as: Nature. 2008 Dec 14;457(7230):687–693. doi: 10.1038/nature07661

Figure 2. Linker controls the oligomerization and activation of Ire1.

Figure 2

a, Observation of visible self-association of Ire1KR32 that can be reversed by salt (NaCl). b, Analytical ultracentrifugation reveals monomers and dimers for Ire1KR as well as dimers and higher-order assemblies for Ire1KR32. Conditions were as in Fig. 1d; open symbols, 13.5 μM Ire1 (20 °C). c, Salt inhibits the RNase activity of Ire1KR32. d, Ire1KR32 has higher RNase activity against HP21 and Xbp1 RNA compared to Ire1KR and Ire1KR24 (Supplementary Fig. 1b; 2). Error bars show variability between single-exponential fits from two to five independent measurements. Conditions similar to those used in Fig. 1d are marked * and **.