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Title
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A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT
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Author
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Abstract
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| 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 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. |
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Language
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English
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Source (journal)
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Nature communications
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Publication
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2019
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ISSN
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2041-1723
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DOI
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10.1038/S41467-019-08865-Z
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Volume/pages
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10
(2019)
, 13 p.
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Article Reference
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972
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ISI
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000459803500008
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Pubmed ID
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30814507
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Medium
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E-only publicatie
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Full text (Publisher's DOI)
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Full text (open access)
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