Fig. 3
From: Structural insights into chaperone addiction of toxin-antitoxin systems

In vivo functions of TA-directed Mtb-SecBTA mutants. a Suppression of Mtb-HigBA1 toxicity by Mtb-SecBTA mutants. E. coli W3110 ΔsecB transformants containing the p29SEN-based Mtb-SecBTA chaperone mutants and pK6-Mtb-HigBA1 were grown to mid-log phase, serially diluted and spotted on LB ampicillin kanamycin agar plates with or without IPTG (to express Mtb-SecBTA) and arabinose (to express Mtb-HigBA1) as indicated. Plates were incubated overnight at 37 °C. Spot tests have been performed in triplicates. b Localization of the mutations on the Mtb-SecBTA/ChAD structure. The molecular surface of the tetramer is represented in light gray. Color coding of interacting residues is the same as in Fig. 1b. Residues that were not tested (i.e., Ala residues and Y146) are colored in pale yellow