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Figure 5 | BMC Microbiology

Figure 5

From: A new suite of tnaA mutants suggests that Escherichia coli tryptophanase is regulated by intracellular sequestration and by occlusion of its active site

Figure 5

D1D3 surface residues that affect polar localization of TnaA-sfGFP. A. Magenta: residues that were not mutagenized. Yellow: alanine substitution mutations that did not affect polar localization of D1D3 or TnaA. Deep blue: mutations that delayed assembly of TnaA foci (mutation sets A2-TnaA, A24-TnaA and A25-TnaA). Cyan: mutations that produced diffuse localization of the D1D3-sfGFP TnaA construct (A9-D1D3). Mutations that produced ovoid foci are not visible in this view and are illustrated in Figure 7. The interfaces between D1D31 and other subunits are illustrated in B to D. Note that mutations causing delayed focus disassembly at stationary phase (Table 3) are not illustrated.

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BMC Microbiology

ISSN: 1471-2180

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