Structural highlights
Publication Abstract from PubMed
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.
CdiA from Enterobacter cloacae Delivers a Toxic Ribosomal RNase into Target Bacteria.,Beck CM, Morse RP, Cunningham DA, Iniguez A, Low DA, Goulding CW, Hayes CS Structure. 2014 May 6;22(5):707-18. doi: 10.1016/j.str.2014.02.012. Epub 2014 Mar, 20. PMID:24657090[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Beck CM, Morse RP, Cunningham DA, Iniguez A, Low DA, Goulding CW, Hayes CS. CdiA from Enterobacter cloacae Delivers a Toxic Ribosomal RNase into Target Bacteria. Structure. 2014 May 6;22(5):707-18. doi: 10.1016/j.str.2014.02.012. Epub 2014 Mar, 20. PMID:24657090 doi:http://dx.doi.org/10.1016/j.str.2014.02.012
