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

Ariel Talavera Perez, Hedvig Tamman, Andres Ainelo, Albert Konijnenberg, San Hadzi, Frank Sobott, Abel Garcia Pino, Rita Horak, Remy Loris

Onderzoeksoutput: Articlepeer review

18 Citaten (Scopus)


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 GraT 2 A 2 complex to the operator. Removal of this region restores operator binding and abrogates GraT toxicity. GraTA represents a TA module where a flexible region in the toxin rather than in the antitoxin controls operon expression and toxin activity.

Originele taal-2English
Pagina's (van-tot)972
Aantal pagina's13
TijdschriftNat Commun
Nummer van het tijdschrift1
StatusPublished - 27 feb 2019


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