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Thioredoxin 1 moonlights as a chaperone for an interbacterial ADP-ribosyltransferase toxin

Author

Listed:
  • Baptiste Dumont

    (Université Libre de Bruxelles (ULB)
    Centre Wallon de Recherches Agronomiques (CRA-W), Bâtiment Emile Marchal)

  • Laurent Terradot

    (Institut de Biologie et Chimie des Protéines (IBCP), Université de Lyon)

  • Eric Cascales

    (Aix-Marseille Université)

  • Laurence Melderen

    (Université Libre de Bruxelles (ULB))

  • Dukas Jurėnas

    (Université Libre de Bruxelles (ULB)
    WEL Research Institute)

Abstract

Formation and breakage of disulfide bridges strongly impacts folding and activity of proteins. Thioredoxin 1 (TrxA) is a small, conserved enzyme that reduces disulfide bonds in the bacterial cytosol. In this study, we provide an example of the emergence of a chaperone role for TrxA, which is independent of redox catalysis. We show that the activity of the secreted bacterial ADP-ribosyltransferase (ART) toxin TreX, which does not contain any cysteines, is dependent on TrxA. TreX binds to the reduced form of TrxA via its carboxy-terminal extension to form a soluble and active complex. Structural studies revealed that TreX-like toxins are homologous to Scabin-like ART toxins which possess cysteine residues and form disulfide bridges at the position that superimposes the TrxA binding site in TreX. Our study therefore suggests that thioredoxin 1 evolved alternative functions by maintaining the interaction with cysteine-free substrates.

Suggested Citation

  • Baptiste Dumont & Laurent Terradot & Eric Cascales & Laurence Melderen & Dukas Jurėnas, 2024. "Thioredoxin 1 moonlights as a chaperone for an interbacterial ADP-ribosyltransferase toxin," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-54892-w
    DOI: 10.1038/s41467-024-54892-w
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    References listed on IDEAS

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    1. Ju-Sim Kim & Alexandra Born & James Karl A. Till & Lin Liu & Sashi Kant & Morkos A. Henen & Beat Vögeli & Andrés Vázquez-Torres, 2022. "Promiscuity of response regulators for thioredoxin steers bacterial virulence," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    2. Sylvie Doublié & Stanley Tabor & Alexander M. Long & Charles C. Richardson & Tom Ellenberger, 1998. "Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution," Nature, Nature, vol. 391(6664), pages 251-258, January.
    3. Christos Gatsogiannis & Felipe Merino & Daniel Roderer & David Balchin & Evelyn Schubert & Anne Kuhlee & Manajit Hayer-Hartl & Stefan Raunser, 2018. "Tc toxin activation requires unfolding and refolding of a β-propeller," Nature, Nature, vol. 563(7730), pages 209-213, November.
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