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Oxidative stress-dependent structural and functional switching of a human 2-Cys peroxiredoxin isotype II that enhances HeLa cell resistance to H2O2-induced cell death.
J Biol Chem. 2005 Aug 05; 280(31):28775-84.JB

Abstract

Although biochemical properties of 2-Cys peroxiredoxins (Prxs) have been extensively studied, their real physiological functions in higher eukaryotic cells remain obscure and certainly warrant further study. Here we demonstrated that human (h) PrxII, a cytosolic isotype of human 2-Cys Prx, has dual functions as a peroxidase and a molecular chaperone, and that these different functions are closely associated with its adoption of distinct protein structures. Upon exposure to oxidative stress, hPrxII assumes a high molecular weight complex structure that has a highly efficient chaperone function. However, the subsequent removal of stressors induces the dissociation of this protein structure into low molecular weight proteins and triggers a chaperone-to-peroxidase functional switch. The formation of a high molecular weight hPrxII complex depends on the hyperoxidation of its N-terminal peroxidatic Cys residue as well as on its C-terminal domain, which contains a "YF motif" that is exclusively found in eukaryotic 2-Cys Prxs. A C-terminally truncated hPrxII exists as low and oligomeric protein species and does not respond to oxidative stress. Moreover, this C-terminal deletion of hPrxII converted it from an oxidation-sensitive to a hyperoxidation-resistant form of peroxidase. When functioning as a chaperone, hPrxII protects HeLa cells from H(2)O(2)-induced cell death, as measured by a terminal deoxynucleotidyltransferase-mediated dUTP nick-end labeling assay and fluorescence-activated cell sorting analysis.

Authors+Show Affiliations

Environmental Biotechnology National Core Research Center, Division of Applied Life Sciences (BK21 Program), Department of Biochemistry, College of Medicine and Institute of Health Sciences, Gyeongsang National University, Jinju 660-701, Korea.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15941719

Citation

Moon, Jeong Chan, et al. "Oxidative Stress-dependent Structural and Functional Switching of a Human 2-Cys Peroxiredoxin Isotype II That Enhances HeLa Cell Resistance to H2O2-induced Cell Death." The Journal of Biological Chemistry, vol. 280, no. 31, 2005, pp. 28775-84.
Moon JC, Hah YS, Kim WY, et al. Oxidative stress-dependent structural and functional switching of a human 2-Cys peroxiredoxin isotype II that enhances HeLa cell resistance to H2O2-induced cell death. J Biol Chem. 2005;280(31):28775-84.
Moon, J. C., Hah, Y. S., Kim, W. Y., Jung, B. G., Jang, H. H., Lee, J. R., Kim, S. Y., Lee, Y. M., Jeon, M. G., Kim, C. W., Cho, M. J., & Lee, S. Y. (2005). Oxidative stress-dependent structural and functional switching of a human 2-Cys peroxiredoxin isotype II that enhances HeLa cell resistance to H2O2-induced cell death. The Journal of Biological Chemistry, 280(31), 28775-84.
Moon JC, et al. Oxidative Stress-dependent Structural and Functional Switching of a Human 2-Cys Peroxiredoxin Isotype II That Enhances HeLa Cell Resistance to H2O2-induced Cell Death. J Biol Chem. 2005 Aug 5;280(31):28775-84. PubMed PMID: 15941719.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Oxidative stress-dependent structural and functional switching of a human 2-Cys peroxiredoxin isotype II that enhances HeLa cell resistance to H2O2-induced cell death. AU - Moon,Jeong Chan, AU - Hah,Young-Sool, AU - Kim,Woe Yeon, AU - Jung,Bae Gyo, AU - Jang,Ho Hee, AU - Lee,Jung Ro, AU - Kim,Sun Young, AU - Lee,Young Mee, AU - Jeon,Min Gyu, AU - Kim,Choong Won, AU - Cho,Moo Je, AU - Lee,Sang Yeol, Y1 - 2005/06/07/ PY - 2005/6/9/pubmed PY - 2005/10/13/medline PY - 2005/6/9/entrez SP - 28775 EP - 84 JF - The Journal of biological chemistry JO - J Biol Chem VL - 280 IS - 31 N2 - Although biochemical properties of 2-Cys peroxiredoxins (Prxs) have been extensively studied, their real physiological functions in higher eukaryotic cells remain obscure and certainly warrant further study. Here we demonstrated that human (h) PrxII, a cytosolic isotype of human 2-Cys Prx, has dual functions as a peroxidase and a molecular chaperone, and that these different functions are closely associated with its adoption of distinct protein structures. Upon exposure to oxidative stress, hPrxII assumes a high molecular weight complex structure that has a highly efficient chaperone function. However, the subsequent removal of stressors induces the dissociation of this protein structure into low molecular weight proteins and triggers a chaperone-to-peroxidase functional switch. The formation of a high molecular weight hPrxII complex depends on the hyperoxidation of its N-terminal peroxidatic Cys residue as well as on its C-terminal domain, which contains a "YF motif" that is exclusively found in eukaryotic 2-Cys Prxs. A C-terminally truncated hPrxII exists as low and oligomeric protein species and does not respond to oxidative stress. Moreover, this C-terminal deletion of hPrxII converted it from an oxidation-sensitive to a hyperoxidation-resistant form of peroxidase. When functioning as a chaperone, hPrxII protects HeLa cells from H(2)O(2)-induced cell death, as measured by a terminal deoxynucleotidyltransferase-mediated dUTP nick-end labeling assay and fluorescence-activated cell sorting analysis. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/15941719/Oxidative_stress_dependent_structural_and_functional_switching_of_a_human_2_Cys_peroxiredoxin_isotype_II_that_enhances_HeLa_cell_resistance_to_H2O2_induced_cell_death_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0021-9258(20)56579-4 DB - PRIME DP - Unbound Medicine ER -