Structural highlights
Function
CNOX_ECOLI Chaperedoxin that combines a chaperone activity with a redox-protective function (PubMed:16563353, PubMed:18657513, PubMed:29754824). Involved in the protection against hypochlorous acid (HOCl), the active ingredient of bleach, which kills bacteria by causing protein aggregation (PubMed:29754824). Functions as an efficient holdase chaperone that protects the substrates of the major folding systems GroEL/GroES and DnaK/DnaJ/GrpE from aggregation. In addition, it prevents the irreversible oxidation of its substrates through the formation of mixed disulfide complexes (PubMed:29754824). After bleach stress, it transfers its substrates to the GroEL/GroES and DnaK/DnaJ/GrpE foldases (PubMed:29754824). Lacks oxidoreductase activity (PubMed:21498507, PubMed:29754824).[1] [2] [3] [4]
References
- ↑ Caldas T, Malki A, Kern R, Abdallah J, Richarme G. The Escherichia coli thioredoxin homolog YbbN/Trxsc is a chaperone and a weak protein oxidoreductase. Biochem Biophys Res Commun. 2006 May 12;343(3):780-6. PMID:16563353 doi:10.1016/j.bbrc.2006.03.028
- ↑ Kthiri F, Le HT, Tagourti J, Kern R, Malki A, Caldas T, Abdallah J, Landoulsi A, Richarme G. The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase. Biochem Biophys Res Commun. 2008 Oct 3;374(4):668-72. PMID:18657513 doi:10.1016/j.bbrc.2008.07.080
- ↑ Lin J, Wilson MA. Escherichia coli Thioredoxin-like Protein YbbN Contains an Atypical Tetratricopeptide Repeat Motif and Is a Negative Regulator of GroEL. J Biol Chem. 2011 Jun 3;286(22):19459-69. Epub 2011 Apr 15. PMID:21498507 doi:10.1074/jbc.M111.238741
- ↑ Goemans CV, Vertommen D, Agrebi R, Collet JF. CnoX Is a Chaperedoxin: A Holdase that Protects Its Substrates from Irreversible Oxidation. Mol Cell. 2018 May 17;70(4):614-627.e7. PMID:29754824 doi:10.1016/j.molcel.2018.04.002
