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A processed noncoding RNA regulates an altruistic bacterial antiviral system

DOI: 10.1038/nsmb.1981 DOI Help
PMID: 21240270 PMID Help

Authors: Tim R. Blower (University of Cambridge) , Xue-yuan Pei (University of Cambridge) , Francesca L. Short (University of Cambridge) , Peter C. Fineran (University of Otago) , David P. Humphreys (UCB) , Ben F. Luisi (Department of Biochemistry, University of Cambridge) , George P. C. Salmond (University of Cambridge)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Structural & Molecular Biology , VOL 18 (2) , PAGES 185–190

State: Published (Approved)
Published: January 2011

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.

Journal Keywords: Bacteriophages; Base; Crystallography; X-Ray; Endoribonucleases; Host-Pathogen; Models; Molecular; Nucleic; Pectobacterium; RNA; Bacterial; RNA; Untranslated

Subject Areas: Biology and Bio-materials

Instruments: I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

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