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. 2012 Oct 4;8(10):e1002958. doi: 10.1371/journal.ppat.1002958

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© 2012 Le et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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(A) Insoluble (ppt) and soluble (sol) fractions of TEP1*S1_cut (lanes 1–2), LRIM1/APL1C (3–4) and TEP1*S1_cut/LRIM1/APL1C (5–6) after 36 h at 20°C. (B) Autolytic cleavage assay (Δ) shows the thioester bond in insoluble TEP1*S1_cut (1) is hydrolyzed while soluble TEP1*S1_cut in complex with LRIM1/APL1C (6) has an intact thioester (heat-induced cleavage of TEP1 C-terminal 85 kDa band). (C) FLAG co-immunoprecipitation of TEP1*R1_cut and TEP1*S1_cut with LRIM1/APL1C after 48 h (TEP1*R1_cut) and 24 h (TEP1*S1_cut), and (D) after 24 days (TEP1*R1_cut). Proteins in both the supernatant (sup) and immunoprecipitated (IP) samples were detected with Western blotting using either α6×His antibody to detect APL1C-6×His and TEP1-6×His C-terminal chain, or αFLAG antibody to detect LRIM1-FLAG/APL1C-FLAG.