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


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-12

AUTHORS

Ariel Talavera, Hedvig Tamman, Andres Ainelo, Albert Konijnenberg, San Hadži, Frank Sobott, Abel Garcia-Pino, Rita Hõrak, Remy Loris

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. More... »

PAGES

972

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41467-019-08865-z

DOI

http://dx.doi.org/10.1038/s41467-019-08865-z

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1112389856

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30814507


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