Fig. 6: Mutating MenA1-MenT1 interaction residues blocks antitoxicity. | Nature Communications

Fig. 6: Mutating MenA1-MenT1 interaction residues blocks antitoxicity.

From: MenT nucleotidyltransferase toxins extend tRNA acceptor stems and can be inhibited by asymmetrical antitoxin binding

Fig. 6

A–C Close-up views of boxed regions from (Fig. 5E), rotated to put MenA1 horizontal, coloured as per (Fig. 5E). D Close-up view of boxed region from (Fig. 5E), coloured as per (Fig. 5E). Black numbers indicate measured bond lengths in Å. E Toxicity and antitoxicity assays were performed in M. smegmatis to study the effect of MenA1 on MenT1. Co-transformants of M. smegmatis containing (i) pGMC-vector (-), MenT1 WT, or MenT1 F28A, F38A or F28A/F38A mutants, and pLAM-vector (-) or MenA1 WT (left panel), or (ii) MenT1 WT, and MenA1 WT, or MenA1 L12R, L14R, V19R, L12R/V19R, L14R/V19R, 1−32 or 1–52 mutants (right panel), were serially diluted and spotted on LB agar plates in the presence or absence of inducers (Atc, 100 ng.ml−1 or Ace, 0.2%). The plates were incubated for 3 days at 37 °C. Representative results of triplicate experiments are shown.

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