A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT

Ariel Talavera (), Hedvig Tamman, Andres Ainelo, Albert Konijnenberg, San Hadži, Frank Sobott, Abel Garcia-Pino, Rita Hõrak and Remy Loris ()
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Ariel Talavera: Vrije Universiteit Brussel
Hedvig Tamman: University of Tartu
Andres Ainelo: University of Tartu
Albert Konijnenberg: Vrije Universiteit Brussel
San Hadži: Vrije Universiteit Brussel
Frank Sobott: University of Antwerp
Abel Garcia-Pino: Université Libre de Bruxelles
Rita Hõrak: University of Tartu
Remy Loris: Vrije Universiteit Brussel

Nature Communications, 2019, vol. 10, issue 1, 1-13

Abstract: Abstract Bacterial toxin-antitoxin (TA) modules are tightly regulated to maintain growth in favorable conditions or growth arrest during stress. A typical regulatory strategy involves the antitoxin binding and repressing its own promoter while the toxin often acts as a co-repressor. Here we show that Pseudomonas putida graTA-encoded antitoxin GraA and toxin GraT differ from other TA proteins in the sense that not the antitoxin but the toxin possesses a flexible region. GraA auto-represses the graTA promoter: two GraA dimers bind cooperatively at opposite sides of the operator sequence. Contrary to other TA modules, GraT is a de-repressor of the graTA promoter as its N-terminal disordered segment prevents the binding of the GraT2A2 complex to the operator. Removal of this region restores operator binding and abrogates Gr aT toxicity. GraTA represents a TA module where a flexible region in the toxin rather than in the antitoxin controls operon expression and toxin activity.

Date: 2019
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DOI: 10.1038/s41467-019-08865-z

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