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. Author manuscript; available in PMC: 2013 Aug 1.
Published in final edited form as: Mol Microbiol. 2012 Jun 12;85(3):445–460. doi: 10.1111/j.1365-2958.2012.08120.x

Fig. 3.

Fig. 3

The YscC secretin causes cytoplasmic membrane permeability to ONPG in a Y. enterocolitica psp null strain.

A. ONPG hydrolysis by whole cells of psp+ (AJD3) and Δpsp (AJD1171) strains containing Φ(catp-lacZ) plasmid pAJD2049 as well as tacp expression plasmids pAJD126 (YscC), pAJD136 (YscC YscW), pAJD633 (AmpE), or pAJD634 (YE0566). Strains had been grown with the indicated concentrations of IPTG for the YscC and YscC YscW panels, with 25 μM IPTG for the AmpE panel, or with 10 μM IPTG for the YE0566 panel. ONPG hydrolysis was monitored by increased absorbance at 420 nm. Readings were normalized so absorbance at 2 min was zero for all samples. Total β-galactosidase activities of cells permeabilized with SDS and chloroform were not significantly different, indicating no differences in β-galactosidase enzyme content (data not shown).

B. Φ(pspAp-lacZ) operon fusion expression in psp+ strain AJD977 containing either pVLT35 (−), pAJD126 (YscC), pAJD136 (YscCW), pAJD633 (AmpE), or pAJD634 (YE0566). Cultures were grown as described in Experimental procedures with 200 μM IPTG (-, YscC and YscCW), 25 μM IPTG (AmpE) or 10μM IPTG (YE0566). Error bars represent one positive standard deviation.