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

Baptiste Dumont, Laurent Terradot, Eric Cascales, Laurence Melderen () and Dukas Jurėnas ()
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Baptiste Dumont: Université Libre de Bruxelles (ULB)
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)

Nature Communications, 2024, vol. 15, issue 1, 1-15

Abstract: 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.

Date: 2024
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DOI: 10.1038/s41467-024-54892-w

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