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  • OER000000774.pdf.jpg
  • Journal article

  • Investigation on the requirements for YbbN/CnoX displaying thiol-disulfide oxidoreductase and chaperone activities

    • Authors : Meireles, Diogo de Abreu; Yokomizo, César Henrique; Netto, Luís Eduardo Soares (-)

  • YbbN/CnoX are proteins that display a Trx domain linked to a tetratricopeptide (TPR) domain, which are involved in protein-protein interactions and protein folding processes. YbbN from Escherichia coli (EcYbbN) displays a co-chaperone (holdase) activity that is induced by HOCl (bleach). EcYbbN contains a SQHC motif within the Trx domain and displays no thiol-disulfide oxidoreductase activity. EcYbbN also presents a second Cys residue at Trx domain (Cys63)...
  • OER000002439.pdf.jpg
  • Ebooks (Sách điện tử)

  • Thioredoxin regulates the redox state and the activity of the human tRNA ligase complex

    • Authors : Jaksch, Dhaarsini (2023)

  • The mammalian tRNA ligase complex (tRNA-LC) catalyzes the splicing of intron-containing pre-tRNAs in the nucleus and the splicing of XBP1 mRNA during the unfolded protein response (UPR) in the cytoplasm. We recently reported that the tRNA-LC co-evolved with PYROXD1, an essential oxidoreductase that protects the catalytic cysteine of RTCB, the catalytic subunit of the tRNA-LC, against aerobic oxidation. In this study we show that the oxidore...