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

Author

Listed:
  • Ariel Talavera

    (Vrije Universiteit Brussel
    Vlaams Instituut voor Biotechnologie)

  • Hedvig Tamman

    (University of Tartu)

  • Andres Ainelo

    (University of Tartu)

  • Albert Konijnenberg

    (Vrije Universiteit Brussel
    Vlaams Instituut voor Biotechnologie
    University of Antwerp)

  • San Hadži

    (Vrije Universiteit Brussel
    University of Ljubljana)

  • Frank Sobott

    (University of Antwerp
    University of Leeds
    University of Leeds)

  • Abel Garcia-Pino

    (Université Libre de Bruxelles)

  • Rita Hõrak

    (University of Tartu)

  • Remy Loris

    (Vrije Universiteit Brussel
    Vlaams Instituut voor Biotechnologie)

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.

Suggested Citation

  • Ariel Talavera & Hedvig Tamman & Andres Ainelo & Albert Konijnenberg & San Hadži & Frank Sobott & Abel Garcia-Pino & Rita Hõrak & Remy Loris, 2019. "A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT," Nature Communications, Nature, vol. 10(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-08865-z
    DOI: 10.1038/s41467-019-08865-z
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    Cited by:

    1. San Hadži & Zala Živič & Matic Kovačič & Uroš Zavrtanik & Sarah Haesaerts & Daniel Charlier & Janez Plavec & Alexander N. Volkov & Jurij Lah & Remy Loris, 2024. "Fuzzy recognition by the prokaryotic transcription factor HigA2 from Vibrio cholerae," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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