Display options
Cite
Dupuy E, Collet JF. Fort CnoX: Protecting Bacterial Proteins From Misfolding and Oxidative Damage. Front Mol Biosci. 2021;8:681932doi: 10.3389/fmolb.2021.681932.
Dupuy, E., & Collet, J. F. (2021). Fort CnoX: Protecting Bacterial Proteins From Misfolding and Oxidative Damage. Frontiers in molecular biosciences, 8681932. https://doi.org/10.3389/fmolb.2021.681932
Dupuy, Emile, and Collet, Jean-François. "Fort CnoX: Protecting Bacterial Proteins From Misfolding and Oxidative Damage." Frontiers in molecular biosciences vol. 8 (2021): 681932. doi: https://doi.org/10.3389/fmolb.2021.681932
Dupuy E, Collet JF. Fort CnoX: Protecting Bacterial Proteins From Misfolding and Oxidative Damage. Front Mol Biosci. 2021 May 04;8:681932. doi: 10.3389/fmolb.2021.681932. eCollection 2021. PMID: 34017858; PMCID: PMC8129009.
Copy Download .nbib Format: NLM
Share it on

Front Mol Biosci. 2021 May 04;8:681932. doi: 10.3389/fmolb.2021.681932. eCollection 2021.

Fort CnoX: Protecting Bacterial Proteins From Misfolding and Oxidative Damage.

Frontiers in molecular biosciences

Emile Dupuy, Jean-François Collet

Affiliations

  1. WELBIO, Brussels, Belgium.
  2. de Duve Institute, Université catholique de Louvain, Brussels, Belgium.

PMID: 34017858 PMCID: PMC8129009 DOI: 10.3389/fmolb.2021.681932

Abstract

How proteins fold and are protected from stress-induced aggregation is a long-standing mystery and a crucial question in biology. Here, we present the current knowledge on the chaperedoxin CnoX, a novel type of protein folding factor that combines holdase chaperone activity with a redox protective function. Focusing on

Copyright © 2021 Dupuy and Collet.

Keywords: CNOX; GroEL and GroES; HOCl; chaperone; holdase; oxidative stress; thioredoxin family proteins

Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

References

  1. J Biol Chem. 2004 May 7;279(19):19486-93 - PubMed
  2. Biochem J. 1998 Jun 15;332 ( Pt 3):617-25 - PubMed
  3. Nat Commun. 2016 Jan 20;7:10357 - PubMed
  4. J Biol Chem. 2013 May 10;288(19):13789-98 - PubMed
  5. Nat Microbiol. 2017 Jan 23;2:16268 - PubMed
  6. Mol Cell. 2005 Feb 4;17(3):381-92 - PubMed
  7. EMBO J. 2004 Jan 14;23(1):160-8 - PubMed
  8. Biochem Biophys Res Commun. 2011 Feb 4;405(1):52-7 - PubMed
  9. J Bacteriol. 1996 Apr;178(7):2131-5 - PubMed
  10. Biochem Biophys Res Commun. 2006 May 12;343(3):780-6 - PubMed
  11. Antioxid Redox Signal. 2010 Oct;13(8):1205-16 - PubMed
  12. Mol Cell. 2014 Mar 6;53(5):689-99 - PubMed
  13. Mol Cell. 2018 May 17;70(4):614-627.e7 - PubMed
  14. Cell Rep. 2012 Mar 29;1(3):251-64 - PubMed
  15. Nat Commun. 2014 Dec 17;5:5804 - PubMed
  16. Biochem Biophys Res Commun. 2008 Oct 3;374(4):668-72 - PubMed
  17. Cell. 2008 Nov 14;135(4):691-701 - PubMed
  18. Cell. 1999 Feb 5;96(3):341-52 - PubMed
  19. Infect Immun. 1987 Oct;55(10):2518-25 - PubMed
  20. J Biol Chem. 2004 May 7;279(19):20529-38 - PubMed
  21. Cell Stress Chaperones. 2011 Jul;16(4):353-67 - PubMed
  22. Cell. 2005 Jul 29;122(2):209-20 - PubMed
  23. J Biol Chem. 2011 Jun 3;286(22):19459-69 - PubMed
  24. Amino Acids. 2003 Dec;25(3-4):259-74 - PubMed
  25. Protein Sci. 2006 Oct;15(10):2217-27 - PubMed
  26. Free Radic Biol Med. 2012 Aug 1;53(3):508-20 - PubMed
  27. Biochim Biophys Acta. 2014 Feb;1840(2):847-75 - PubMed
  28. F1000Res. 2019 Sep 23;8: - PubMed
  29. mBio. 2018 Nov 27;9(6): - PubMed

Publication Types