Thioredoxin 1 moonlights as a chaperone for an interbacterial ADP-ribosyltransferase toxin
Thioredoxin 1 moonlights as a chaperone for an interbacterial ADP-ribosyltransferase toxin
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London: Nature Publishing Group UK
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English
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London: Nature Publishing Group UK
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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...
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Thioredoxin 1 moonlights as a chaperone for an interbacterial ADP-ribosyltransferase toxin
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TN_cdi_doaj_primary_oai_doaj_org_article_afead9ac7c6c4a9d9c7b7c15f4e0e4a6
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_afead9ac7c6c4a9d9c7b7c15f4e0e4a6
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ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-024-54892-w
