CdiA from Enterobacter cloacae delivers a toxic ribosomal RNase into target bacteria

Structure
Christina M BeckChristopher S Hayes

Abstract

Contact-dependent growth inhibition (CDI) is one mechanism of inter-bacterial competition. CDI(+) cells export large CdiA effector proteins, which carry a variety of C-terminal toxin domains (CdiA-CT). CdiA-CT toxins are specifically neutralized by cognate CdiI immunity proteins to protect toxin-producing cells from autoinhibition. Here, we use structure determination to elucidate the activity of a CDI toxin from Enterobacter cloacae (ECL). The structure of CdiA-CT(ECL) resembles the C-terminal nuclease domain of colicin E3, which cleaves 16S ribosomal RNA to disrupt protein synthesis. In accord with this structural homology, we show that CdiA-CT(ECL) uses the same nuclease activity to inhibit bacterial growth. Surprisingly, although colicin E3 and CdiA(ECL) carry equivalent toxin domains, the corresponding immunity proteins are unrelated in sequence, structure, and toxin-binding site. Together, these findings reveal unexpected diversity among 16S rRNases and suggest that these nucleases are robust and versatile payloads for a variety of toxin-delivery platforms.

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Citations

Aug 26, 2015·Proceedings of the National Academy of Sciences of the United States of America·Julia L E WillettChristopher S Hayes
Jun 4, 2014·Molecular Microbiology·Christina M BeckChristopher S Hayes
Oct 10, 2015·Journal of Molecular Biology·Robert P MorseCelia W Goulding
Sep 22, 2015·Journal of Molecular Biology·Julia L E WillettChristopher S Hayes
Jul 3, 2015·Molecular Microbiology·Zachary C RuheChristopher S Hayes
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