Unknown

Dataset Information

0

A processed noncoding RNA regulates an altruistic bacterial antiviral system.


ABSTRACT: The ? 10³? 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.

SUBMITTER: Blower TR 

PROVIDER: S-EPMC4612426 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

A processed noncoding RNA regulates an altruistic bacterial antiviral system.

Blower Tim R TR   Pei Xue Y XY   Short Francesca L FL   Fineran Peter C PC   Humphreys David P DP   Luisi Ben F BF   Salmond George P C GP  

Nature structural & molecular biology 20110116 2


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 reso  ...[more]

Similar Datasets

| S-EPMC9477407 | biostudies-literature
| S-EPMC8513474 | biostudies-literature
| S-EPMC4895142 | biostudies-literature
| S-EPMC7390449 | biostudies-literature
| S-EPMC8326114 | biostudies-literature
| S-SCDT-EMBOJ-2018-100041 | biostudies-other
| S-EPMC4550694 | biostudies-literature
| S-EPMC9780829 | biostudies-literature
| S-EPMC5893147 | biostudies-literature
| S-EPMC5320610 | biostudies-other