Peroxiredoxins (Prxs) are a recently discovered family of antioxidant enzymes that catalyze the reduction of peroxides and alkyl peroxides. In this study, four Prx genes (named as ThPrxII, ThPrxIIE, ThPrxIIF, and Th2CysPrx) were cloned from Tamarix hispida. Their expression profiles in response to stimulus of NaCl, NaHCO 3, PEG, CdCl 2 and abscisic acid (ABA) in roots, stems and leaves of T. hispida were investigated using real-time RT-PCR. The results showed that the four ThPrxs were all expressed in roots, stems and leaves. Furthermore, the transcript levels of ThPrxIIE and ThPrxII were the lowest and the highest, respectively, in all tissue types. All the ThPrx genes were induced by both NaCl and NaHCO 3 and reached their highest expression levels at the onset of stress in roots. Under PEG and CdCl 2 stress, the expression patterns of these ThPrxs showed temporal and spatial specificity. The expressions of the ThPrxs were all differentially regulated by ABA, indicating that they are all involved in the ABA signaling pathway. These findings reveal a complex regulation of Prxs that is dependent on the type of Prx, tissue, and the signaling molecule. The divergence of the stress-dependent transcriptional regulation of the ThPrx gene family in T. hispida may provide an essential basis for the elucidation of Prx function in future work.
References
[1]
Stacy, R.A.; Munthe, E.; Steinum, T.; Sharma, B.; Aalen, R.B. A peroxiredoxin antioxidant is encoded by a dormancy related gene, Per1, expressed during late development in the aleurone and embryo of barley grains. Plant Mol. Biol 1996, 31, 1205–1216.
[2]
Baier, M.; Dietz, K.J. Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases. Plant Mol. Biol 1996, 31, 553–564.
[3]
Pulido, P.; Spínola, M.C.; Kirchsteiger, K.; Guinea, M.; Pascual, M.B.; Sahrawy, M.; Sandalio, L.M.; Dietz, K.J.; González, M.; Cejudo, F.J. Functional analysis of the pathways for 2-Cys peroxiredoxin reduction in Arabidopsis thaliana chloroplasts. J. Exp. Bot 2010, 61, 4043–4054.
[4]
Umate, P. Genome-wide analysis of thioredoxin fold superfamily peroxiredoxins in Arabidopsis and rice. Plant Signal Behav 2010, 5, 1543–1546.
[5]
Horling, F.; Baier, M.; Dietz, K.J. Redox-regulation of the expression of the peroxide- detoxifying chloroplast 2-cys peroxiredoxin in the liverwort Riccia. fluitans. Planta 2001, 214, 304–313.
[6]
Baier, M.; Dietz, K.J. The plant 2-Cys peroxiredoxin BAS1 is a nuclear-encoded chloroplast protein: its expressional regulation, phylogenetic origin, and implications for its specific physiological function in plants. Plant J 1997, 12, 179–190.
[7]
Rouhier, N.; Gelhaye, E.; Sautiere, P.E.; Brun, A.; Laurent, P.; Tagu, D.; Gerard, J.; de Fay, E.; Meyer, Y.; Jacquot, J.P. Isolation and characterization of a new peroxiredoxin from poplar sieve tubes that uses either glutaredoxin or thioredoxin as a proton donor. Plant Physiol 2001, 127, 1299–1309.
[8]
Kiba, A.; Nishihara, M.; Tsukatani, N.; Nakatsuka, T.; Kato, Y.; Yamamura, S. A peroxiredoxin Q homolog from gentians is involved in both resistance against fungal disease and oxidative stress. Plant Cell Physiol 2005, 46, 1007–1015.
[9]
Berberich, T.; Uebler, M.; Feierabend, J. Cloning of a cDNA encoding a thioredoxin peroxidase (TPx) homolog from winter rye (Secale cereale L.) (Accession No. AF076920) (PGR98-167). Plant Physiol 1998, 118, 711.
[10]
Bréhélin, C.; Meyer, E.H.; de Souris, J.P.; Bonnard, G.; Meyer, Y. Resemblance and dissemblance of Arabidopsis type II peroxiredoxins: similar sequences for divergent gene expression, protein localization, and activity. Plant Physiol 2003, 132, 2045–2057.
[11]
Kim, M.D.; Kim, Y.H.; Kwon, S.Y.; Jang, B.Y.; Lee, S.Y.; Yun, D.J.; Cho, J.H.; Kwak, S.S.; Lee, H.S. Overexpression of 2-cysteine peroxiredoxin enhances tolerance to methyl viologen-mediated oxidative stress and high temperature in potato plants. Plant Physiol. Biochem 2011, 49, 891–897.
[12]
Finkemeier, I.; Goodman, M.; Lamkemeyer, P.; Kandlbinder, A.; Sweetlove, L.J.; Dietz, K.J. The mitochondrial type II peroxiredoxin F is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress. J. Biol. Chem 2005, 280, 12168–12180.
[13]
Haslek？s, C.; Viken, M.K.; Grini, P.E.; Nygaard, V.; Nordgard, S.H.; Meza, T.J.; Aalen, R.B. Seed 1-cysteine peroxiredoxin antioxidants are not involved in dormancy, but contribute to inhibition of germination during stress. Plant Physiol 2003, 133, 1148–1157.
[14]
Lee, K.O.; Jang, H.H.; Jung, B.G.; Chi, Y.H.; Lee, J.Y.; Choi, Y.O.; Lee, J.R.; Lim, C.O.; Cho, M.J.; Lee, S.Y. Rice 1Cys-peroxiredoxin over-expressed in transgenic tobacco does not maintain dormancy but enhances antioxidant activity. FEBS Lett. 2000, 486, 103–106.
[15]
Kim, S.Y.; Jang, H.H.; Lee, J.R.; Sung, N.R.; Lee, H.B.; Lee, D.H.; Park, D.J.; Kang, C.H.; Chung, W.S.; Lim, C.O.; et al. Oligomerization and chaperone activity of a plant 2-Cys peroxiredoxin in response to oxidative stress. Plant Sci 2009, 177, 227–232.
[16]
Kim, S.Y.; Paeng, S.K.; Nawkar, G.M.; Maibam, P.; Lee, E.S.; Kim, K.S.; Lee, D.H.; Park, D.J.; Kang, S.B.; Kim, M.R.; et al. The 1-Cys peroxiredoxin, a regulator of seed dormancy, functions as a molecular chaperone under oxidative stress conditions. Plant Sci 2011, 181, 119–124.
[17]
Jing, L.W.; Chen, S.H.; Guo, X.L.; Zhang, H.; Zhao, Y.X. Overexpression of a chloroplast-located peroxiredoxin Q gene, SsPrxQ, increases the salt and low-temperature tolerance of Arabidopsis. J. Integr. Plant Biol 2006, 48, 1244–1249.
[18]
Kim, K.H.; Alam, I.; Lee, K.W.; Sharmin, S.A.; Kwak, S.S.; Lee, S.Y.; Lee, B.H. Enhanced tolerance of transgenic tall fescue plants overexpressing 2-Cys peroxiredoxin against methyl viologen and heat stresses. Biotechnol Lett 2010, 32, 571–576.
[19]
Muthuramalingam, M.; Seidel, T.; Laxa, M.; Nunes de Miranda, S.M.; G？rtner, F.; Str？her, E.; Kandlbinder, A.; Dietz, K.J. Multiple redox and non-redox interactions define 2-Cys peroxiredoxin as a regulatory hub in the chloroplast. Mol. Plant. 2009, 2, 1273–1288.
[20]
Dietz, K.J. Peroxiredoxins in Plants and Cyanobacteria. Antioxid. Redox Signal 2011, 15, 1129–1159.
[21]
Mowla, S.B.; Thomson, J.A.; Farrant, J.M.; Mundree, S.G. A novel stress-inducible antioxidant enzyme identified from the resurrection plant Xerophyta viscosa Baker. Planta 2002, 215, 716–726.
[22]
Horling, F.; Lamkemeyer, P.; K？nig, J.; Finkemeier, I.; Kandlbinder, A.; Baier, M.; Dietz, K.J. Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis. Plant Physiol 2003, 131, 317–325.
[23]
Barranco-Medina, S.; Krell, T.; Bernier-Villamor, L.; Sevilla, F.; Lazaro, J.J.; Dietz, K.J. Hexameric oligomerization of mitochondrial peroxiredoxin PrxIIF and formation of an ultrahigh affinity complex with its electron donor thioredoxin Trx-o. J. Exp. Bot 2008, 59, 3259–3269.
[24]
Haslek？s, C.; Grini, P.E.; Nordgard, S.H.; Thorstensen, T.; Viken, M.K.; Nygaard, V.; Aalen, R.B. ABI3 mediates expression of the peroxiredoxin antioxidant AtPER1 gene and induction by oxidative stress. Plant Mol. Biol 2003, 53, 313–326.
[25]
Baier, M.; Str？her, E.; Dietz, K.J. The acceptor availability at photosystem I and ABA control nuclear expression of 2-Cys peroxiredoxin-A in Arabidopsis thaliana. Plant Cell Physiol 2004, 45, 997–1006.
[26]
Gao, C.; Wang, Y.; Liu, G.; Yang, C.; Jiang, J.; Li, H. Expression profiling of salinity-alkali stress responses by large-scale expressed sequence tag analysis in Tamarix hispid. Plant Mol. Biol. 2008, 66, 245–258.
[27]
Li, H.; Wang, Y.; Jiang, J.; Liu, G.; Gao, C.; Yang, C. Identification of genes responsive to salt stress on Tamarix hispida roots. Gene 2009, 433, 65–71.
[28]
Livak, K.J.; Schmittgen, T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(？Delta Delta C(T)) Method. Methods 2001, 25, 402–408.
