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

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 regio

SUBMITTER: Talavera A 

PROVIDER: S-EPMC6393540 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature