A.Talavera
et al.
(2019).
A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT.
Nat Commun,
10,
972.
PubMed id: 30814507
DOI: 10.1038/s41467-019-08865-z
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.