The peroxiredoxin gene family in Drosophila melanogaster

被引:145
作者
Radyuk, SN
Klichko, VI
Spinola, B
Sohal, RS
Orr, WC
机构
[1] So Methodist Univ, Dept Biol Sci, Dallas, TX 75275 USA
[2] Univ So Calif, Dept Mol Pharmacol & Toxicol, Los Angeles, CA USA
关键词
antioxidant enzymes; peroxiredoxin; thioredoxin peroxidase; oxidative stress; free radicals;
D O I
10.1016/S0891-5849(01)00692-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Five peroxiredoxin genes have been identified in Drosophila melanogaster on the basis of a genome-wide search. Three of the genes (DPx-4156, DPx-4783, and DPx-5037) fall into the 2-Cys subgroup, while the other two (DPx-2540 and DPx-6005) belong to the 1-Cys subgroup. Using cDNAs, all five were expressed in E. coli and the purified recombinant proteins were shown to reduce H2O2 in the presence of dithiothreitol. ne three 2-Cys Prx were also shown to be active in the thioredoxin system and were, consequently, classified as thioredoxin peroxidases. Antisera raised against the DPx-4783 recombinant protein crossreacted with all family members and recognized protein species of the predicted sizes (22-27 kD). All five family members, when individually overexpressed. in Drosophila S2 cells, conferred some resistance to H2O2 treatment, as measured by cell viability. Functional diversification of the Drosophila peroxiredoxin family members was suggested by two lines of evidence: (i) the patterns of mRNA accumulation varied for the different genes during development and (ii) recombinant proteins fused to an epitope tag and overexpressed in Drosophila cells, differed in subcellular localizations-three proteins occurred in the cytosol, one was localized to the mitochondria, and one was found to be secreted. (C) 2001 Elsevier Science Inc.
引用
收藏
页码:1090 / 1100
页数:11
相关论文
共 40 条
[21]   Peroxiredoxin IV is a secretable protein with heparin-binding properties under reduced conditions [J].
Okado-Matsumoto, A ;
Matsumoto, A ;
Fujii, J ;
Taniguchi, N .
JOURNAL OF BIOCHEMISTRY, 2000, 127 (03) :493-501
[22]   Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae [J].
Park, SG ;
Cha, MK ;
Jeong, W ;
Kim, IH .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (08) :5723-5732
[23]   Novel 28-kDa secretory protein from rat olfactory epithelium [J].
Peshenko, IV ;
Novoselov, VI ;
Evdokimov, VA ;
Nikolaev, YV ;
Shuvaeva, TM ;
Lipkin, VM ;
Fesenko, EE .
FEBS LETTERS, 1996, 381 (1-2) :12-14
[24]  
PROSPERI MT, 1993, J BIOL CHEM, V268, P11050
[25]  
RHEE SG, 1994, MOL CELLS, V4, P137
[26]   Polypeptides differentially expressed in imaginal discs define the peroxiredoxin family of genes in Drosophila [J].
Rodriguez, J ;
Agudo, M ;
Van Damme, J ;
Vandekerckhove, J ;
Santarén, JF .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2000, 267 (02) :487-497
[27]   Fasciola hepatica:: Heterologous expression and functional characterization of a thioredoxin peroxidase [J].
Salazar-Calderón, M ;
Martín-Alonso, JM ;
de Eguino, ADR ;
Casais, R ;
Marín, MS ;
Parra, F .
EXPERIMENTAL PARASITOLOGY, 2000, 95 (01) :63-70
[28]  
Sambrook J., 2002, MOL CLONING LAB MANU
[29]   Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 Å resolution [J].
Schröder, E ;
Littlechild, JA ;
Lebedev, AA ;
Errington, N ;
Vagin, AA ;
Isupov, MN .
STRUCTURE, 2000, 8 (06) :605-615
[30]   Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily [J].
Schröder, E ;
Ponting, CP .
PROTEIN SCIENCE, 1998, 7 (11) :2465-2468