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. 2014 Aug 8;9(8):e103774. doi: 10.1371/journal.pone.0103774

Figure 3. MALT1 undergoes auto-proteolysis in vitro.

Figure 3

A) Features of F-STII-MALT1 and LZ-MALT1. F: Flag epitope, STII: StrepII-tag, 6H: 6-Histidine tag, LZ: Leuzine zipper. B) Top: In vitro cleavage of the fluorogenic tetratpeptide substrate Ac-LVSR-AMC (50 µM) by F-STII-MALT1 in increasing concentrations of the cosmotropic salt NH4-citrate (0.2, 0.4, 0.6, and 0.8 M M), by F-STII-MALT1 in 0.8M NH4-citrate buffer in the presence of the MALT1 protease inhibitors z-VRPR-fmk (10 µM) and z-LVSR-fmk (10 µM) and by LZ-MALT1 or LZ-MALT1-C464A in 0.8 M NH M NH4-citrate buffer. The barchart shows cleavage activity as Fluorescence Units (FU) increase/min. Results are expressed as means ± SD (n = 3). Bottom: enzymatic reactions were analysed by immunoblotting with a-MALT1-C, a-p76 neo-epitope and a-MALT1-N.