Fig. 8: CdiA-CT processing is independent of the proton gradient and inner-membrane receptors. | Nature Communications

Fig. 8: CdiA-CT processing is independent of the proton gradient and inner-membrane receptors.

From: Proteolytic processing induces a conformational switch required for antibacterial toxin delivery

Fig. 8

a CdiA-CT processing. Inhibitor cells that deploy CdiA-CTEC3006 or CdiA-CTYm43969 were mixed at a 1:1 ratio with target bacteria of the indicated genotypes. Urea-soluble protein was isolated from co-cultures for immunoblot analysis using polyclonal antisera to the N-terminal TPS domain of CdiA. b In vivo nuclease activity. Total RNA was isolated from the co-cultures in panel a for Northern blot analysis using probes to tRNAIle and tRNAGlu. c Inhibitor cells that deploy CdiA-CTEC3006 or CdiA-CTYm43969 were mixed at a 1:1 ratio with target bacteria in the absence or presence of carbonyl cyanide m-chlorophenylhydrazone (CCCP). Urea-soluble protein was analyzed by immunoblotting with polyclonal antisera to the N-terminal TPS transport domain of CdiA. d In vivo nuclease activity. Total RNA was isolated from the co-cultures in panel c for Northern blot analysis using probes to tRNAIle and tRNAGlu. The experiment in panel a was repeated independently three times with similar results. The experiments in panels b–d were performed twice independently with similar results. Source data are provided as a Source Data file.

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