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. Author manuscript; available in PMC: 2015 Jul 1.
Published in final edited form as: Mol Microbiol. 2014 Jun 15;93(2):276–290. doi: 10.1111/mmi.12658

Figure 5. The N-terminal domain of CdiA-CT536 is sufficient for import.

Figure 5

A) Colicin E5 is composed of translocation, receptor-binding and nuclease domains. The C-terminal domain (ColE5-CT) has anticodon nuclease activity. The NT536-CTE5 protein contains residues Val3016 – Gly3097 of CdiA536 fused to the ColE5-CT nuclease domain. B) E. coli XL-1 cells were treated with purified ColE5-CT or NT536-CTE5 fusion at 30 min (indicated by the arrow) and growth monitored by OD600 measurements. Where indicated, cells carried plasmid-borne cdiI536 (cdiI536) or imE5 immunity genes. C) Northern blot analysis of toxin-treated cells. Total RNA was isolated from the cells in panel B and tRNATyr analyzed by northern blot. The migration positions of full-length and cleaved tRNATyr are indicated.