Chaperone activity with a redox switch - PubMed (original) (raw)
Chaperone activity with a redox switch
U Jakob et al. Cell. 1999.
Free article
Abstract
Hsp33, a member of a newly discovered heat shock protein family, was found to be a very potent molecular chaperone. Hsp33 is distinguished from all other known molecular chaperones by its mode of functional regulation. Its activity is redox regulated. Hsp33 is a cytoplasmically localized protein with highly reactive cysteines that respond quickly to changes in the redox environment. Oxidizing conditions like H2O2 cause disulfide bonds to form in Hsp33, a process that leads to the activation of its chaperone function. In vitro and in vivo experiments suggest that Hsp33 protects cells from oxidants, leading us to conclude that we have found a protein family that plays an important role in the bacterial defense system toward oxidative stress.
Similar articles
- Activation of the redox-regulated chaperone Hsp33 by domain unfolding.
Graf PC, Martinez-Yamout M, VanHaerents S, Lilie H, Dyson HJ, Jakob U. Graf PC, et al. J Biol Chem. 2004 May 7;279(19):20529-38. doi: 10.1074/jbc.M401764200. Epub 2004 Mar 15. J Biol Chem. 2004. PMID: 15023991 - Activation of the redox-regulated molecular chaperone Hsp33--a two-step mechanism.
Graumann J, Lilie H, Tang X, Tucker KA, Hoffmann JH, Vijayalakshmi J, Saper M, Bardwell JC, Jakob U. Graumann J, et al. Structure. 2001 May 9;9(5):377-87. doi: 10.1016/s0969-2126(01)00599-8. Structure. 2001. PMID: 11377198 - Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone.
Barbirz S, Jakob U, Glocker MO. Barbirz S, et al. J Biol Chem. 2000 Jun 23;275(25):18759-66. doi: 10.1074/jbc.M001089200. J Biol Chem. 2000. PMID: 10764757 - Redox-regulated molecular chaperones.
Graf PC, Jakob U. Graf PC, et al. Cell Mol Life Sci. 2002 Oct;59(10):1624-31. doi: 10.1007/pl00012489. Cell Mol Life Sci. 2002. PMID: 12475172 Free PMC article. Review. - Oxidative stress: Protein folding with a novel redox switch.
Ruddock LW, Klappa P. Ruddock LW, et al. Curr Biol. 1999 Jun 3;9(11):R400-2. doi: 10.1016/s0960-9822(99)80253-x. Curr Biol. 1999. PMID: 10359689 Review.
Cited by
- The role of metals in hypothiocyanite resistance in Escherichia coli.
Gray MJ. Gray MJ. J Bacteriol. 2024 Aug 22;206(8):e0009824. doi: 10.1128/jb.00098-24. Epub 2024 Jul 17. J Bacteriol. 2024. PMID: 39016617 - Single-molecule mechanical studies of chaperones and their clients.
Rief M, Žoldák G. Rief M, et al. Biophys Rev (Melville). 2022 Oct 13;3(4):041301. doi: 10.1063/5.0098033. eCollection 2022 Dec. Biophys Rev (Melville). 2022. PMID: 38505517 Free PMC article. Review. - The role of metals in hypothiocyanite resistance in Escherichia coli.
Gray MJ. Gray MJ. bioRxiv [Preprint]. 2024 Mar 8:2024.03.07.583962. doi: 10.1101/2024.03.07.583962. bioRxiv. 2024. PMID: 38496647 Free PMC article. Updated. Preprint. - Evidence that protein thiols are not primary targets of intracellular reactive oxygen species in growing Escherichia coli.
Eben SS, Imlay JA. Eben SS, et al. Front Microbiol. 2023 Dec 13;14:1305973. doi: 10.3389/fmicb.2023.1305973. eCollection 2023. Front Microbiol. 2023. PMID: 38152379 Free PMC article. - The cold atmospheric pressure plasma-generated species superoxide, singlet oxygen and atomic oxygen activate the molecular chaperone Hsp33.
Dirks T, Krewing M, Vogel K, Bandow JE. Dirks T, et al. J R Soc Interface. 2023 Oct;20(207):20230300. doi: 10.1098/rsif.2023.0300. Epub 2023 Oct 25. J R Soc Interface. 2023. PMID: 37876273 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases