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. Author manuscript; available in PMC: 2012 Jun 1.
Published in final edited form as: Biochim Biophys Acta. 2011 Feb 18;1808(6):1709–1715. doi: 10.1016/j.bbamem.2011.02.006

Figure 2. The L-selectin TM domain lacks the ability to self-associate in the cell membrane.

Figure 2

(A) Sequence of the L-selectin TM domain. Residue numbers marking the sequences analyzed by the TOXCAT assay are labeled on the top. (B) MalE complementation test showing correct topology of chimeric ToxR’-TM-MBP proteins. Each L-selectin TM sequence tested in the assay is identified by its starting and ending residue numbers as in the mature protein. On M9 minimum media, where maltose is the only carbon source, only cells with MBP expression in the periplasm survive. MalE-deficient MM39 E. coli cells transformed with pMal-c2 and pMal-p2 vectors (New England Biolabs), which express MBP in the cytoplasm and the periplasm, respectively, were included as controls. (C) The enzymatic activity of CAT induced by self-association of the tested L-selectin TM sequences and expressed as the percentage of that induced by GpA-WT. The GpA-WT and GpA-G83I constructs were used as positive and negative controls, respectively. The data are shown as mean ± s.d. of 3 independent measurements. The lower panel shows the expression levels of the chimeric protein probed by Western blot against MBP.