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Nat Commun ; 13(1): 5078, 2022 08 29.
Article in English | MEDLINE | ID: mdl-36038560

ABSTRACT

Many Gram-negative bacteria use CdiA effector proteins to inhibit the growth of neighboring competitors. CdiA transfers its toxic CdiA-CT region into the periplasm of target cells, where it is released through proteolytic cleavage. The N-terminal cytoplasm-entry domain of the CdiA-CT then mediates translocation across the inner membrane to deliver the C-terminal toxin domain into the cytosol. Here, we show that proteolysis not only liberates the CdiA-CT for delivery, but is also required to activate the entry domain for membrane translocation. Translocation function depends on precise cleavage after a conserved VENN peptide sequence, and the processed ∆VENN entry domain exhibits distinct biophysical and thermodynamic properties. By contrast, imprecisely processed CdiA-CT fragments do not undergo this transition and fail to translocate to the cytoplasm. These findings suggest that CdiA-CT processing induces a critical structural switch that converts the entry domain into a membrane-translocation competent conformation.


Subject(s)
Escherichia coli Proteins , Anti-Bacterial Agents/metabolism , Anti-Bacterial Agents/pharmacology , Escherichia coli/metabolism , Escherichia coli Proteins/metabolism , Membrane Proteins/metabolism , Proteolysis
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