Molecular structure and function of the novel BrnT/BrnA toxin-antitoxin system of Brucella abortus.

The Journal of Biological Chemistry
Brook E HeatonSean Crosson

Abstract

Type II toxin-antitoxin (TA) systems are expressed from two-gene operons that encode a cytoplasmic protein toxin and its cognate protein antitoxin. These gene cassettes are often present in multiple copies on bacterial chromosomes, where they have been reported to regulate stress adaptation and persistence during antimicrobial treatment. We have identified a novel type II TA cassette in the intracellular pathogen Brucella abortus that consists of the toxin gene, brnT, and its antitoxin, brnA. BrnT is coexpressed and forms a 2:2 tetrameric complex with BrnA, which neutralizes BrnT toxicity. The BrnT(2)-BrnA(2) tetramer binds its own promoter via BrnA, and autorepresses its expression; its transcription is strongly induced in B. abortus by various stressors encountered by the bacterial cell during infection of a mammalian host. Although highly divergent at the primary sequence level, an atomic resolution (1.1 Å) crystal structure of BrnT reveals a secondary topology related to the RelE family of type II ribonuclease toxins. However, overall tertiary structural homology to other RelE family toxins is low. A functional characterization of BrnT by site-directed mutagenesis demonstrates a correspondence between its in vitro activity ...Continue Reading

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