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Convergent Evolution of the Barnase/EndoU/Colicin/RelE (BECR) Fold in Antibacterial tRNase Toxins. | LitMetric

Convergent Evolution of the Barnase/EndoU/Colicin/RelE (BECR) Fold in Antibacterial tRNase Toxins.

Structure

Biomolecular Science and Engineering Program, University of California, Santa Barbara, CA, USA; Department of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, CA, USA. Electronic address:

Published: November 2019

AI Article Synopsis

Article Abstract

Contact-dependent growth inhibition (CDI) is a form of interbacterial competition mediated by CdiB-CdiA two-partner secretion systems. CdiA effector proteins carry polymorphic C-terminal toxin domains (CdiA-CT), which are neutralized by specific CdiI immunity proteins to prevent self-inhibition. Here, we present the crystal structures of CdiA-CT⋅CdiI complexes from Klebsiella pneumoniae 342 and Escherichia coli 3006. The toxins adopt related folds that resemble the ribonuclease domain of colicin D, and both are isoacceptor-specific tRNases that cleave the acceptor stem of deacylated tRNA. Although the toxins are similar in structure and substrate specificity, CdiA-CT activity requires translation factors EF-Tu and EF-Ts, whereas CdiA-CT is intrinsically active. Furthermore, the corresponding immunity proteins are unrelated in sequence and structure. CdiI forms a dimeric β sandwich, whereas CdiI is an α-solenoid monomer. Given that toxin-immunity genes co-evolve as linked pairs, these observations suggest that the similarities in toxin structure and activity reflect functional convergence.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6834915PMC
http://dx.doi.org/10.1016/j.str.2019.08.010DOI Listing

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