Fig. S1. The protein structure of the MARTX types I (approximately 5200 aa), II (approximately 4700 aa) and III (approximately 4600 aa). The external regions, the repeats (vertical lines) and the internal domains for each toxin are colour coded as indicated at the bottom. The putative domains are: RID, Rho-GTPase inactivation; HCR, highly conserved regions; CPD, autocatalytic cysteine protease; DUF, domain with an unknown function; ACD, actin cross-linking; á/β, á/β hydrolase; rtx PA, rtxA of Photorhabdus asymbiotica; Efa1/LifA, lymphostatin. Diagrams are drawn to scale. Figure adapted from Roig and colleagues (2011).


Fig. S2. Confirmation of various rtxA13 mutants.

A. The gene structure of rtxA13. The coding region is indicated by an arrow. A 1816 bp DNA fragment between the two HindIII sites that contains part of the putative ACD domain (5886–7269 bp) was deleted to generate the rtxA13 mutants. The probe used in southern hybridization is indicated below.

B. Southern hybridization analysis of the mutants. The plasmid DNA (P) or total DNA (G) was digested with BglII, separated in a 0.8% agarose gel, and probed with a DNA fragment amplified from rtxA13 with primers RTX5 (5′-GAAACACGCAAAGCCGATGC-3′) and RTX16 (5′-CTCATCTCTGAGTGGAAGCC-3′). CECT4999: wild-type; CT302: ΔcrtxA13; CT284: ΔprtxA13; CT285: ΔcrtxA13ΔprtxA13. The bands derived from rtxA13 with and without deletions (2.6 and 4.4 kb, respectively) are indicated. M: 1 kb plus DNA markers.

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