期刊
NATURE COMMUNICATIONS
卷 10, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-019-08865-z
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资金
- Fonds voor Wetenschappelijk Onderzoek Vlaanderen [G.0135.15N, G0C1213N, G.0090.11N]
- Onderzoeksraad of the Vrije Universiteit Brussel [OZR2232, SPR13]
- European Community's Seventh Framework Programme (FP7/2007-2013) under BioStruct-X [1673, 6131]
- Hercules Foundation [UABR/11/012]
- Estonian Research Council [PUT1351, IUT20-19]
- Slovenian Research Agency [P1-0201, J1-5448]
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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