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. 2010 Apr 21;285(25):19668–19687. doi: 10.1074/jbc.M110.122598

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© 2010 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 4. — Secondary structure predictions and localization of His₁₀-WbbM. A, sequence and predicted secondary structure of WbbM outlining β-sheets (black arrows) and α-helices (black boxes). The GT-8 region (residues 284–549) is identified, as is a putative linked region that may separate two independent domains (WbbM^N and WbbM^C). B, localization of His₁₀-WbbM (expressed from pWQ522 in E. coli CWG286), His₁₀-WbbM^N (pWQ530), and His₁₀-WbbM^C (pWQ531). Cell-free lysates (S12) were separated into soluble (S100) and membrane-containing (P100) fractions and the His-tagged proteins were detected in Western immunoblots using mouse anti-His₅ monoclonal antibody followed by goat anti-mouse horseradish peroxidase-conjugated antibody. Loading was standardized to the original cell suspension (prior to lysis), allowing direct visual assessment of the cellular distribution of His₁₀-WbbM.