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Yeast thioredoxin peroxidase expression enhances the resistance of Escherichia coli to oxidative stress induced by singlet oxygen.
Redox Rep. 2002; 7(2):79-84.RR

Abstract

Singlet oxygen ((1)O(2)) is a highly reactive form of molecular oxygen that may harm living systems by oxidizing critical cellular macromolecules. A soluble protein from Saccharomyces cerevisiae specifically provides protection against a thiol-containing metal-catalyzed oxidation system (thiol/Fe(3+)/O(2)) but not against an oxidation system without thiol. This 25 kDa protein acts as a peroxidase but requires the NADPH-dependent thioredoxin system or a thiol-containing intermediate, and was named thioredoxin peroxidase (TPx). The role of TPx in the cellular defense against oxidative stress induced by singlet oxygen was investigated in Escherichia coli containing an expression vector with a yeast genomic DNA fragment that encodes TPx and mutant in which the catalytically essential amino acid cysteine (Cys-47) has been replaced with alanine by a site-directed mutagenesis. Upon exposure to methylene blue and visible light, which generates singlet oxygen, there was a distinct difference between the two strains in regard to growth kinetics, viability, the accumulation of oxidized proteins and lipids, and modulation of activities of superoxide dismutase and catalase. The results suggest that TPx may play an important protective role in a singlet oxygen-mediated cellular damage.

Authors+Show Affiliations

Department of Biochemistry, College of Natural Sciences, Kyungpook National University, Taegu 702-701, Korea.No affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

12189053

Citation

Kim, Sun Yee, et al. "Yeast Thioredoxin Peroxidase Expression Enhances the Resistance of Escherichia Coli to Oxidative Stress Induced By Singlet Oxygen." Redox Report : Communications in Free Radical Research, vol. 7, no. 2, 2002, pp. 79-84.
Kim SY, Kim EJ, Park JW. Yeast thioredoxin peroxidase expression enhances the resistance of Escherichia coli to oxidative stress induced by singlet oxygen. Redox Rep. 2002;7(2):79-84.
Kim, S. Y., Kim, E. J., & Park, J. W. (2002). Yeast thioredoxin peroxidase expression enhances the resistance of Escherichia coli to oxidative stress induced by singlet oxygen. Redox Report : Communications in Free Radical Research, 7(2), 79-84.
Kim SY, Kim EJ, Park JW. Yeast Thioredoxin Peroxidase Expression Enhances the Resistance of Escherichia Coli to Oxidative Stress Induced By Singlet Oxygen. Redox Rep. 2002;7(2):79-84. PubMed PMID: 12189053.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Yeast thioredoxin peroxidase expression enhances the resistance of Escherichia coli to oxidative stress induced by singlet oxygen. AU - Kim,Sun Yee, AU - Kim,Eun Ju, AU - Park,Jeen-Woo, PY - 2002/8/22/pubmed PY - 2003/2/14/medline PY - 2002/8/22/entrez SP - 79 EP - 84 JF - Redox report : communications in free radical research JO - Redox Rep VL - 7 IS - 2 N2 - Singlet oxygen ((1)O(2)) is a highly reactive form of molecular oxygen that may harm living systems by oxidizing critical cellular macromolecules. A soluble protein from Saccharomyces cerevisiae specifically provides protection against a thiol-containing metal-catalyzed oxidation system (thiol/Fe(3+)/O(2)) but not against an oxidation system without thiol. This 25 kDa protein acts as a peroxidase but requires the NADPH-dependent thioredoxin system or a thiol-containing intermediate, and was named thioredoxin peroxidase (TPx). The role of TPx in the cellular defense against oxidative stress induced by singlet oxygen was investigated in Escherichia coli containing an expression vector with a yeast genomic DNA fragment that encodes TPx and mutant in which the catalytically essential amino acid cysteine (Cys-47) has been replaced with alanine by a site-directed mutagenesis. Upon exposure to methylene blue and visible light, which generates singlet oxygen, there was a distinct difference between the two strains in regard to growth kinetics, viability, the accumulation of oxidized proteins and lipids, and modulation of activities of superoxide dismutase and catalase. The results suggest that TPx may play an important protective role in a singlet oxygen-mediated cellular damage. SN - 1351-0002 UR - https://www.unboundmedicine.com/medline/citation/12189053/Yeast_thioredoxin_peroxidase_expression_enhances_the_resistance_of_Escherichia_coli_to_oxidative_stress_induced_by_singlet_oxygen_ L2 - https://www.tandfonline.com/doi/full/10.1179/135100002125000307 DB - PRIME DP - Unbound Medicine ER -