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A processed noncoding RNA regulates an altruistic bacterial antiviral system

Nature Structural & Molecular Biology volume 18, pages 185–190 (2011)Cite this article

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Abstract

The ≥1030 bacteriophages on Earth relentlessly drive adaptive coevolution, forcing the generation of protective mechanisms in their bacterial hosts. One such bacterial phage-resistance system, ToxIN, consists of a protein toxin (ToxN) that is inhibited in vivo by a specific RNA antitoxin (ToxI); however, the mechanisms for this toxicity and inhibition have not been defined. Here we present the crystal structure of the ToxN–ToxI complex from Pectobacterium atrosepticum, determined to 2.75-Å resolution. ToxI is a 36-nucleotide noncoding RNA pseudoknot, and three ToxI monomers bind to three ToxN monomers to generate a trimeric ToxN–ToxI complex. Assembly of this complex is mediated entirely through extensive RNA-protein interactions. Furthermore, a 2′-3′ cyclic phosphate at the 3′ end of ToxI, and catalytic residues, identify ToxN as an endoRNase that processes ToxI from a repetitive precursor but is regulated by its own catalytic product.

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Figure 1: Overview of TA systems.
Figure 2: ToxIN complex structure.
Figure 3: ToxI pseudoknot structure.
Figure 4: ToxN has an endoRNase active site.
Figure 5: Identification of ToxN–ToxI residues that are vital for toxicity and interaction.
Figure 6: Structural comparisons in the ToxN family.

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  • 28 January 2011

    In the version of this article initially published online, there was a mistake in the cell dimension values in row 3 of Table 1 (SeMet). These should read 182.85, 118.13, 41.90. The error has been corrected in all versions of the article.

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Acknowledgements

We thank the beamline scientists at station ID23.1 in the European Synchrotron Research Facility, Grenoble, France, and at stations I03 and I04 in the Diamond Light Source, Oxford, UK. This work was supported by grants from the Biotechnology and Biological Sciences Research Council (UK), the Wellcome Trust (UK) and the Marsden Fund, Royal Society of New Zealand. Work with P. atrosepticum was performed under a plant health license from the Department for Environment, Food and Rural Affairs (UK). T.R.B. was supported by a Collaborative Award in Science and Engineering Studentship from UCB Ltd. F.L.S. was supported by a Commonwealth Scholarship from the Commonwealth Scholarships Commission (UK).

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Authors and Affiliations

  1. Department of Biochemistry, University of Cambridge, Cambridge, UK

    Tim R Blower, Xue Y Pei, Francesca L Short, Ben F Luisi & George P C Salmond

  2. Department of Microbiology and Immunology, University of Otago, Dunedin, New Zealand

    Peter C Fineran

  3. UCB, Slough, Berkshire, UK

    David P Humphreys

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Contributions

T.R.B., X.Y.P., F.L.S. and B.F.L. conducted experiments and analyzed data, with input from G.P.C.S. Experiments were designed by T.R.B., X.Y.P., P.C.F., B.F.L. and G.P.C.S. All authors interpreted experiments and contributed to writing the paper.

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Correspondence to George P C Salmond.

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Blower, T., Pei, X., Short, F. et al. A processed noncoding RNA regulates an altruistic bacterial antiviral system. Nat Struct Mol Biol 18, 185–190 (2011). https://doi.org/10.1038/nsmb.1981

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