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Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae.
J Biol Chem. 2000 Feb 25; 275(8):5723-32.JB

Abstract

A new type of peroxidase ("thiol peroxidase"; TPx) having cysteine as the primary site of catalysis has been discovered from prokaryotes to eukaryotes. In addition to two yeast TPx isoforms (TSA I and TSA II/AHPC1) previously described, three additional TPx homologues were identified by analysis of the open reading frame data base for Saccharomyces cerevisiae. Three novel isoforms showed a distinct thiol peroxidase activity supported by thioredoxin, and appeared to be distinctively localized in cytoplasm, mitochondria, and nucleus. Each isoform was named after its subcellular localization such as cytoplasmic TPx I (cTPx I or TSA I), cTPx II, cTPx III (TSA II/AHPC1), mitochondrial TPx (mTPx), and nuclear TPx (nTPx). Their transcriptional activities suggest that cTPx I and cTPx III are the most predominant isoforms among the five type isoforms. Transcriptional activities of TPx isoenzymes during yeast life span were quite different from each other. Unlike other TPx null mutants, cTPx I null mutant was hypersensitive to various oxidants except for 4-nitroquinoline N-oxide. The null mutant was more resistant toward 4-nitroquinoline N-oxide and acidic culture than its wild type. The severe growth retardation of cTPx II mutant resulted in accumulation of G(1)-phased cells. Based on kinetic properties of five isoforms, their subcellular localizations, and distinct physiology of each null mutant, we discussed the physiological functions of five types of TPx isoenzymes in yeast throughout the full growth cycle.

Authors+Show Affiliations

National Creative Research Initiatives Center for Antioxidant Proteins, Department of Biochemistry, Paichai University, Taejon 302-735, Korea.No 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

10681558

Citation

Park, S G., et al. "Distinct Physiological Functions of Thiol Peroxidase Isoenzymes in Saccharomyces Cerevisiae." The Journal of Biological Chemistry, vol. 275, no. 8, 2000, pp. 5723-32.
Park SG, Cha MK, Jeong W, et al. Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae. J Biol Chem. 2000;275(8):5723-32.
Park, S. G., Cha, M. K., Jeong, W., & Kim, I. H. (2000). Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae. The Journal of Biological Chemistry, 275(8), 5723-32.
Park SG, et al. Distinct Physiological Functions of Thiol Peroxidase Isoenzymes in Saccharomyces Cerevisiae. J Biol Chem. 2000 Feb 25;275(8):5723-32. PubMed PMID: 10681558.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae. AU - Park,S G, AU - Cha,M K, AU - Jeong,W, AU - Kim,I H, PY - 2000/2/22/pubmed PY - 2000/4/1/medline PY - 2000/2/22/entrez SP - 5723 EP - 32 JF - The Journal of biological chemistry JO - J Biol Chem VL - 275 IS - 8 N2 - A new type of peroxidase ("thiol peroxidase"; TPx) having cysteine as the primary site of catalysis has been discovered from prokaryotes to eukaryotes. In addition to two yeast TPx isoforms (TSA I and TSA II/AHPC1) previously described, three additional TPx homologues were identified by analysis of the open reading frame data base for Saccharomyces cerevisiae. Three novel isoforms showed a distinct thiol peroxidase activity supported by thioredoxin, and appeared to be distinctively localized in cytoplasm, mitochondria, and nucleus. Each isoform was named after its subcellular localization such as cytoplasmic TPx I (cTPx I or TSA I), cTPx II, cTPx III (TSA II/AHPC1), mitochondrial TPx (mTPx), and nuclear TPx (nTPx). Their transcriptional activities suggest that cTPx I and cTPx III are the most predominant isoforms among the five type isoforms. Transcriptional activities of TPx isoenzymes during yeast life span were quite different from each other. Unlike other TPx null mutants, cTPx I null mutant was hypersensitive to various oxidants except for 4-nitroquinoline N-oxide. The null mutant was more resistant toward 4-nitroquinoline N-oxide and acidic culture than its wild type. The severe growth retardation of cTPx II mutant resulted in accumulation of G(1)-phased cells. Based on kinetic properties of five isoforms, their subcellular localizations, and distinct physiology of each null mutant, we discussed the physiological functions of five types of TPx isoenzymes in yeast throughout the full growth cycle. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/10681558/Distinct_physiological_functions_of_thiol_peroxidase_isoenzymes_in_Saccharomyces_cerevisiae_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0021-9258(18)30604-5 DB - PRIME DP - Unbound Medicine ER -