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. Author manuscript; available in PMC: 2020 Nov 5.
Published in final edited form as: Structure. 2019 Sep 9;27(11):1660–1674.e5. doi: 10.1016/j.str.2019.08.010

Figure 7. The nuclease active sites of CdiA-CTKp342 and CdiA-CTEC3006.

Figure 7.

A) Superimposition of CdiA-CTKp342 onto the nuclease domain of colicin D. B) Putative active sites of CdiA-CTKp342 and CdiA-CTEC3006 nuclease domains. C & D) Competition co-cultures. Target bacteria were co-cultured at a 1:1 ratio with inhibitor cells that deliver the indicated CdiA-CTKp342 (panel C) or CdiA-CTEC3006 (panel D) variants. Competitive indices are calculated as the ratio of viable target to inhibitor cells at 1 h divided by the initial ratio. Data are from three independent experiments together with the average ± SEM. See also Figure S4. E & F) Toxin activities in co-cultures. Inhibitor strains were co-cultured with the indicated target cells for 30 min, then total RNA was isolated for Northern blot analysis. G) In vitro nuclease activity of CdiA-CTEC3006 variants. The indicated CdiA-CTEC3006 domains were purified and incubated with deacylated tRNA substrate.