Fig. 4: Complementation of the FY mutant with orthologous TerC proteins. | Nature Communications

Fig. 4: Complementation of the FY mutant with orthologous TerC proteins.

From: TerC proteins function during protein secretion to metalate exoenzymes

Fig. 4

a Phylogenetic tree (branch lengths in red) comparing TerC proteins from B. subtilis (BsuMeeF, BsuMeeY) with homologs from Listeria monocytogenes (lmo0991, lmo0992) and B. anthracis (BanTerC). Protein sequences were aligned by MUSCLE (MUltiple Sequence Comparison by Log-Expectation)106 using online analysis tools from EMBL-EBI107. The Newick data was then manipulated by Interactive Tree Of Life (iTOL) to display phylogenetic tree108. Scale bar = 0.1. Leaf nodes are shown as black circles and internal nodes are displayed as black squares (b) Colony sizes of FY mutant with induction of TerC proteins on LB medium with 50 µM IPTG as measured by imageJ. Isolated colonies from three independent cultures were measured for each strain and data are presented as mean ± standard deviation. P value of each strain compared to FY samples was calculated using Welch’s t test, two-tailed, ****p < 0.0001. Sample size for each strain: WT, n = 55; FY, n = 40; FY Pspac(hy)-meeF, n = 49; FY Pspac(hy)-meeY, n = 56; FY Pspac(hy)-lmo0991, n = 50; FY Pspac(hy)-lmo0992, n = 66; FY Pspac(hy)-banTerC, n = 48. c Protease activities of FY mutant strains with expression of TerC proteins as measured on 5% milk agar plates. Cells were grown in LB broth with 50 µM IPTG inducer to OD600 0.4 and 2 µl of serially diluted cells (100–10-5) were inoculated on the plates followed by incubation at 37 °C for 24 h. The image is representative of three independent experiments. Source data are provided as a Source Data file.

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