ArticleNature communications2024
Thioredoxin 1 moonlights as a chaperone for an interbacterial ADP-ribosyltransferase toxin.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Disulphide maintenance systems and proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- A type VI secretion ADP-ribosyltransferase Rhs toxin selectively modifies charged tRNAThr(GGU) anticodon loops to block ACC codon decoding.Nucleic acids research · 2026Article
- An ART-fold Rhs toxin from Pluralibacter gergoviae defines Tne5, a novel family of NAD(P) glycohydrolases effectors.The Journal of biological chemistry · 2026Article
- Elongation Factor Tu Acts as a Chaperone to Activate an Antibacterial RNase Toxin.Molecular microbiology · 2026Article
- An interbacterial cysteine protease toxin inhibits cell growth by targeting type II DNA topoisomerases GyrB and ParE.PLoS biology · 2025Article
- The Type VI Secretion System of Sinorhizobium fredii USDA257 Is Required for Successful Nodulation With Glycine max cv Pekin.Microbial biotechnology · 2025Article
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Authors and funding
5 authors.
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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.
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