Abstract
The plants get exposed to different abiotic stresses and pathogen attack due to their sessile nature. These stresses result in the overproduction of reactive oxygen species (ROS) such as superoxide radical (O2·−), hydrogen peroxide (H2O2), singlet oxygen (ˡO2) etc. To overcome the effect of these ROS, different classes of antioxidants are involved in providing tolerance to plants. The superoxide dismutase (SOD) consists of one such major class of antioxidant proteins, which provide primary defense against different stress conditions. These are ubiquitous metalloenzymes, which carry out the dismutation of superoxide radicals (O ·−2 ) into molecular oxygen and hydrogen peroxide (H2O2). In plants, a total of three classes of SODs are reported i.e., Cu-ZnSODs, FeSODs, and MnSODs, which have cytoplasmic or apoplastic or nuclear, chloroplastic and mitochondrial subcellular localization, respectively. SODs are well known for their role in plant growth and development and in providing tolerance against biotic and abiotic stress conditions by combating oxidative stress. These enzymes are stable and active over a broad range of pH and temperature. Due to their astonishing enzymatic properties, they are widely used in industries for various purposes. In this chapter, we have focused on the myriad functions of SODs in response to biotic and abiotic stresses and their utilization in enhancing the stress tolerance in plants.
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References
Ahmad P, John R, Sarwat D, Umar S (2008) Responses of proline, lipid peroxidation and antioxidative enzymes in two varieties of Pisum sativum L. under salt stress. Int J Plant Prod 2(4)
Alexieva V, Sergiev I, Mapelli S, Karanov E (2001) The effect of drought and ultraviolet radiation on growth and stress markers in pea and wheat. Plant, Cell Environ 24:1337–1344. https://doi.org/10.1046/j.1365-3040.2001.00778.x
Alharby HF, Metwali EMR, Fuller MP, Aldhebiani AY (2016) The alteration of mRNA expression of SOD and GPX genes, and proteins in tomato (Lycopersicon esculentum Mill) under stress of NaCl and/or ZnO nanoparticles. Saudi J Biol Sci 23:773–781. https://doi.org/10.1016/j.sjbs.2016.04.012
Almeselmani M, Deshmukh PS, Sairam RK, Kushwaha SR, Singh TP (2006) Protective role of antioxidant enzymes under high temperature stress. Plant Sci 171:382–388. https://doi.org/10.1016/J.PLANTSCI.2006.04.009
Alscher RG, Erturk N, Heath LS (2002) Role of superoxide dismutases (SODs) in controlling oxidative stress in plants. J Exp Bot 53:1331–1341. https://doi.org/10.1093/jexbot/53.372.1331
Anjum NA, Umar S, Iqbal M, Khan NA (2011) Cadmium causes oxidative stress in mung bean by affecting the antioxidant enzyme system and ascorbate-glutathione cycle metabolism. Russ J Plant Physiol 58:92–99. https://doi.org/10.1134/S1021443710061019
Apel K, Hirt H (2004) Reactive oxygen species: metabolism, oxidative stress, and signal transduction. Annu Rev Plant Biol 55:373–399. https://doi.org/10.1146/annurev.arplant.55.031903.141701
Arora P, Bhardwaj R, Kanwar MK (2012) Effect of 24-epibrassinolide on growth, protein content and antioxidative defense system of Brassica juncea L. subjected to cobalt ion toxicity. Acta Physiol Plant 34:2007–2017. https://doi.org/10.1007/s11738-012-1002-2
ASADA K (1987) Production and scavenging of active oxygen in photosynthesis. Photoinhibition 227–287
Ashraf M, Ali Q (2008) Relative membrane permeability and activities of some antioxidant enzymes as the key determinants of salt tolerance in canola (Brassica napus L.). Environ Exp. Bot 63:266–273. https://doi.org/10.1016/j.envexpbot.2007.11.008
Bafana A, Dutt S, Kumar S, Ahuja PS (2011) Superoxide dismutase: an industrial perspective. Crit Rev Biotechnol 31:65–76. https://doi.org/10.3109/07388551.2010.490937
Baldensperger JB (1978) An iron-containing superoxide dismutase from the chemolithotrophic Thiobacillus denitrificans? RT? strain. Arch Microbiol 119:237–244. https://doi.org/10.1007/BF00405401
Bannister WH, Bannister JV, Barra D, Bond J, Bossa F (1991) Evolutionary aspects of superoxide dismutase: the copper/zinc enzyme. Free Radic Res Commun 12–13(Pt 1):349–361
Barna B, Fodor J, Pogány M, Király Z (2003) Role of reactive oxygen species and antioxidants in plant disease resistance. Pest Manag Sci 59:459–464. https://doi.org/10.1002/ps.706
Benavides MP, Gallego SM, Tomaro ML (2005) Cadmium toxicity in plants. Brazilian J Plant Physiol 17:21–34. https://doi.org/10.1590/S1677-04202005000100003
Blankenship RE (2010) Early evolution of photosynthesis. Plant Physiol 154:434–438. https://doi.org/10.1104/pp.110.161687
Bor M, Özdemir F, Türkan I (2003) The effect of salt stress on lipid peroxidation and antioxidants in leaves of sugar beet Beta vulgaris L. and wild beet Beta maritima L Plant Sci 164:77–84. https://doi.org/10.1016/s0168-9452(02)00338-2
Bordo D, Djinovic K, Bolognesi M (1994) Conserved patterns in the Cu, Zn superoxide dismutase family. J Mol Biol 238:366–386. https://doi.org/10.1006/jmbi.1994.1298
Bowler C, Slooten L, Vandenbranden S, De Rycke R, Botterman J, Sybesma C, Van Montagu M, Inzé D (1991) Manganese superoxide dismutase can reduce cellular damage mediated by oxygen radicals in transgenic plants. EMBO J 10:1723–1732
Bowler C, Montagu MV, Inze D (1992) Superoxide dismutase and stress tolerance. Annu Rev Plant Physiol Plant Mol Biol 43:83–116 (1992). https://doi.org/10.1146/annurev.pp.43.060192.000503
Bresson-Rival D, Boivin P, Linden G, Perrier E, Humbert G (1997) Stabilized compositions of superoxide dismutase obtained from germinated plant seeds. US Pat. 5904921
Cannon RE, White JA, Scandalios JG (1987) Cloning of cDNA for maize superoxide dismutase 2 (SOD2). Proc Natl Acad Sci 84:179–183. https://doi.org/10.1073/pnas.84.1.179
Carter C, Thornburg RW (2000) Tobacco Nectarin I. J Biol Chem 275:36726–36733. https://doi.org/10.1074/jbc.M006461200
Cekic FO, Ünyayar S, Keleş Y, Çekiç FÖ (2006) The antioxidative response of two tomato species with different drought tolerances as a result of drought and cadmium stress combinations. Plant Soil Environ 51. https://doi.org/10.17221/3556-pse
Ceylan HA, Türkan I, Sekmen AH (2013) Effect of coronatine on antioxidant enzyme response of chickpea roots to combination of PEG-induced osmotic stress and heat stress. J Plant Growth Regul 32:72–82. https://doi.org/10.1007/s00344-012-9277-5
Chaitanya KV, Sundar D, Masilamani S, Ramachandra Reddy A (2002) Variation in heat stress-induced antioxidant enzyme activities among three mulberry cultivars. Plant Growth Regul 36:175–180. https://doi.org/10.1023/A:1015092628374
Chen Z, Pan YH, An LY, Yang WJ, Xu LG, Zhu C (2013) Heterologous expression of a halophilic archaeon manganese superoxide dismutase enhances salt tolerance in transgenic rice. Russ J Plant Physiol 60:359–366. https://doi.org/10.1134/S1021443713030059
Cho Park (2000) Mercury-induced oxidative stress in tomato seedlings. Plant Sci 156:1–9
Cho U-H, Seo N-H (2005) Oxidative stress in Arabidopsis thaliana exposed to cadmium is due to hydrogen peroxide accumulation. Plant Sci 168:113–120. https://doi.org/10.1016/J.PLANTSCI.2004.07.021
Colin C, N’Guyen Q (1999) Cosmetic composition containing, in combination, a superoxide-dismutase and a melanin pigment. US Pat. 5925363
Colin C, N’Guyen QL (2007) Composition including superoxide dismutase and prickly-pear cactus for minimizing and preventing hangovers. US Pat. 5925363 (2007)
Crowell DN, Amasino RM (1991) Induction of Specific mRNAs in cultured soybean cells during cytokinin or auxin starvation. Plant Physiol 95:711–715. https://doi.org/10.1104/pp.95.3.711
Deeba F, Pandey AK, Ranjan S, Mishra A, Singh R, Sharma YK, Shirke PA, Pandey V (2012) Physiological and proteomic responses of cotton (Gossypium herbaceum L.) to drought stress. Plant Physiol Biochem 53:6–18 (2012). https://doi.org/10.1016/j.plaphy.2012.01.002
del Río LA, Sandalio LM, Palma JM, Bueno P, Corpas FJ (1992) Metabolism of oxygen radicals in peroxisomes and cellular implications. Free Radic Biol Med 13:557–580
Diwan H, Khan I, Ahmad A, Iqbal M (2010) Induction of phytochelatins and antioxidant defence system in Brassica juncea and Vigna radiata in response to chromium treatments. Plant Growth Regul 61:97–107. https://doi.org/10.1007/s10725-010-9454-0
Dixit V, Pandey V, Shyam R (2001) Differential antioxidative responses to cadmium in roots and leaves of pea (Pisum sativum L. cv. Azad)1. J Exp Bot 52:1101–1109 (2001). https://doi.org/10.1093/jexbot/52.358.1101
Doupis G, Bertaki M, Psarras G, Kasapakis I, Chartzoulakis K (2013) Water relations, physiological behavior and antioxidant defence mechanism of olive plants subjected to different irrigation regimes. Sci Hortic (Amsterdam) 153:150–156. https://doi.org/10.1016/J.SCIENTA.2013.02.010
Elstner FE (1991) Metabolisms of oxygen activation in different compartments of plant cells. Act Oxyg Stress Plant Metab 13–25 (1991)
Faize M, Burgos L, Faize L, Petri C, Barba-Espin G, Díaz-Vivancos P, Clemente-Moreno MJ, Alburquerque N, Hernandez JA (2012) Modulation of tobacco bacterial disease resistance using cytosolic ascorbate peroxidase and Cu. Zn-superoxide dismutase Plant Pathol 61:858–866. https://doi.org/10.1111/j.1365-3059.2011.02570.x
Fan J, Hu Z, Xie Y, Chan Z, Chen K, Amombo E, Chen L, Fu J (2015) Alleviation of cold damage to photosystem II and metabolisms by melatonin in Bermudagrass. Front Plant Sci 6:925. https://doi.org/10.3389/fpls.2015.00925
Feng X, Lai Z, Lin Y, Lai G, Lian C (2015) Genome-wide identification and characterization of the superoxide dismutase gene family in Musa acuminata cv. Tianbaojiao (AAA group). BMC Genomics 16:823. https://doi.org/10.1186/s12864-015-2046-7
Feng K, Yu J, Cheng Y, Ruan M, Wang R, Ye Q, Zhou G, Li Z, Yao Z, Yang Y, Zheng Q, Wan H (2016) The SOD gene family in tomato: identification, phylogenetic relationships, and expression patterns. Front Plant Sci 7:1279. https://doi.org/10.3389/fpls.2016.01279
Filiz E, Tombuloğlu H (2015) Genome-wide distribution of superoxide dismutase (SOD) gene families inSorghum bicolor. TURKISH J Biol 39:49–59. https://doi.org/10.3906/biy-1403-9
Fink RC, Scandalios JG (2002) Molecular evolution and structure–function relationships of the superoxide dismutase gene families in angiosperms and their relationship to other eukaryotic and prokaryotic superoxide dismutases. Arch Biochem Biophys 399:19–36. https://doi.org/10.1006/abbi.2001.2739
Foyer CH, Noctor G (2009) Redox regulation in photosynthetic organisms: signaling, acclimation, and practical implications. Antioxid Redox Signal 11:861–905. https://doi.org/10.1089/ars.2008.2177
Fridovich I (1986) Superoxide dismutases. Adv Enzymol Relat Areas Mol Biol 58:61–97
Getzoff ED, Cabelli DE, Fisher CL, Parge HE, Viezzoli MS, Banci L, Hallewell RA (1992) Faster superoxide dismutase mutants designed by enhancing electrostatic guidance. Nature 358:347–351. https://doi.org/10.1038/358347a0
Gill SS, Tuteja N (2010) Reactive oxygen species and antioxidant machinery in abiotic stress tolerance in crop plants. Plant Physiol Biochem 48:909–930. https://doi.org/10.1016/j.plaphy.2010.08.016
Gomez JM, Jimenez A, Olmos E, Sevilla F (2003) Location and effects of long-term NaCl stress on superoxide dismutase and ascorbate peroxidase isoenzymes of pea (Pisum sativum cv. Puget) chloroplasts. J Exp Bot 55:119–130 (2003). https://doi.org/10.1093/jxb/erh013
Govrin EM, Levine A (2000) The hypersensitive response facilitates plant infection by the necrotrophic pathogen Botrytis cinerea. Curr Biol 10:751–757
Gucciardo S, Wisniewski J-P, Brewin NJ, Bornemann S (2007) A germin-like protein with superoxide dismutase activity in pea nodules with high protein sequence identity to a putative rhicadhesin receptor. J Exp Bot 58:1161–1171. https://doi.org/10.1093/jxb/erl282
Gueta-Dahan Y, Yaniv Z, Zilinskas BA, Ben-Hayyim G (1997) Salt and oxidative stress: similar and specific responses and their relation to salt tolerance in Citrus. Planta 203:460–469. https://doi.org/10.1007/s004250050215
Gupta AS, Heinen JL, Holaday AS, Burke JJ, Allen RD (1993) Increased resistance to oxidative stress in transgenic plants that overexpress chloroplastic Cu/Zn superoxide dismutase. Proc Natl Acad Sci U S A 90:1629–1633. https://doi.org/10.1073/pnas.90.4.1629
Halliwell B (2006) Reactive species and antioxidants. Redox biology is a fundamental theme of aerobic life. Plant Physiol 141:312–322. https://doi.org/10.1104/pp.106.077073
Hans RK, Agrawal N, Verma K, Misra RB, Ray RS, Farooq M (2008) Assessment of the phototoxic potential of cosmetic products. Food Chem Toxicol 46:1653–1658. https://doi.org/10.1016/J.FCT.2008.01.005
Harinasut P, Poonsopa D, Roengmongkol K, Charoensataporn R (2003) Salinity effects on antioxidant enzymes in mulberry cultivar. Sci. Asia 29:109–113. https://doi.org/10.2306/scienceasia1513-1874.2003.29.109
Hediye Sekmen A, Türkan İ, Takio S (2007) Differential responses of antioxidative enzymes and lipid peroxidation to salt stress in salt-tolerant Plantago maritima and salt-sensitive Plantago media. Physiol Plant 131:399–411. https://doi.org/10.1111/j.1399-3054.2007.00970.x
Hernandez J, Olmos E, Corpas F, Sevilla F, Del Río L (1995) Salt-induced oxidative stress in chloroplasts of pea plants. Plant Sci 105:151–167. https://doi.org/10.1016/0168-9452(94)04047-8
Hernández JA, Del Río LA, Sevilla F (1994) Salt stress-induced changes in superoxide dismutase isozymes in leaves and mesophyll protoplasts from Vigna unguiculata (L.) Walp New Phytol 126:37–44. https://doi.org/10.1111/j.1469-8137.1994.tb07527.x
Hersh T, Hersh R (2002) Antioxidants to neutralize tobacco free radicals. US Pat. 6415798
Hsu YT, Kao CH (2004) Cadmium toxicity is reduced by nitric oxide in rice leaves. Plant Growth Regul 42:227–238. https://doi.org/10.1023/B:GROW.0000026514.98385.5c
Hu X, Hao C, Cheng Z-M, Zhong Y (2019) Genome-wide identification, characterization, and expression analysis of the grapevine superoxide dismutase (SOD) family. Int J Genomics 2019:1–13. https://doi.org/10.1155/2019/7350414
Huang M, Guo Z (2005) Responses of antioxidative system to chilling stress in two rice cultivars differing in sensitivity. Biol Plant 49:81–84. https://doi.org/10.1007/s00000-005-1084-3
Israr M, Sahi S, Datta R, Sarkar D (2006) Bioaccumulation and physiological effects of mercury in Sesbania drummondii. Chemosphere 65:591–598. https://doi.org/10.1016/j.chemosphere.2006.02.016
Jebara S, Jebara M, Limam F, Aouani ME (2005) Changes in ascorbate peroxidase, catalase, guaiacol peroxidase and superoxide dismutase activities in common bean (Phaseolus vulgaris) nodules under salt stress. J Plant Physiol 162:929–936. https://doi.org/10.1016/j.jplph.2004.10.005
Jiang Y, Huang B (2001) Drought and heat stress injury to two cool-season turfgrasses in relation to antioxidant metabolism and lipid peroxidation. Crop Sci—Crop SCI 41. https://doi.org/10.2135/cropsci2001.412436x
Kanematsu S, Asada K (1978) Superoxide dismutase from an anaerobic photosynthetic bacterium Chromatium vinosum. Arch Biochem Biophys 185:473–482. https://doi.org/10.1016/0003-9861(78)90191-1
Kanematsu S, Asada K (1990) Characteristic amino acid sequences of chloroplast and cytosol isozymes of CuZn-superoxide dismutase in Spinach. Rice and Horsetail Plant Cell Physiol 31:99–112. https://doi.org/10.1093/oxfordjournals.pcp.a077887
Kang G, Wang C, Sun G, Wang Z (2003) Salicylic acid changes activities of H2O2-metabolizing enzymes and increases the chilling tolerance of banana seedlings. Environ Exp Bot 50:9–15. https://doi.org/10.1016/S0098-8472(02)00109-0
Karuppanapandian T, Moon JC, Kim C, Manoharan K, Kim W (2011) Reactive oxygen species in plants: their generation, signal transduction, and scavenging mechanisms. Aust J Crop Sci 5:709–725
Kasai T, Suzuki T, Ono K, Ogawa K, Inagaki Y, Ichinose Y, Toyoda K, Shiraishi T (2006) Pea extracellular Cu/Zn-superoxide dismutase responsive to signal molecules from a fungal pathogen. J Gen Plant Pathol 72:265–272. https://doi.org/10.1007/s10327-006-0283-y
Khan MH, Panda SK (2002) Induction of oxidative stress in roots of oryza sativa L. Response to Salt Stress Biol Plant 45:625–627. https://doi.org/10.1023/A:1022356112921
Khanna-Chopra R, Sabarinath S (2004) Heat-stable chloroplastic Cu/Zn superoxide dismutase in Chenopodium murale. Biochem Biophys Res Commun 320:1187–1192. https://doi.org/10.1016/j.bbrc.2004.06.071
Kim FJ, Kim HP, Hah YC, Roe JH (1996) Differential expression of superoxide dismutases containing Ni and Fe/Zn in Streptomyces coelicolor. Eur J Biochem 241:178–185
Kirby TW, Lancaster JR, Fridovich I (1981) Isolation and characterization of the iron-containing superoxide dismutase of Methanobacterium bryantii. Arch Biochem Biophys 210:140–148
Kliebenstein DJ, Monde RA, Last RL (1998) Superoxide dismutase in Arabidopsis: an eclectic enzyme family with disparate regulation and protein localization. Plant Physiol 118:637–650
Kochhar S, Kochhar VK (2008) Identification and characterization of a super-stable Cu–Zn SOD from leaves of turmeric (Curcuma longa L.). Planta 228:307–318. https://doi.org/10.1007/s00425-008-0738-9
Kotak S, Larkindale J, Lee U, von Koskull-Döring P, Vierling E, Scharf K-D (2007) Complexity of the heat stress response in plants. Curr Opin Plant Biol 10:310–316. https://doi.org/10.1016/j.pbi.2007.04.011
Kumar D, Yusuf MA, Singh P, Sardar M, Sarin NB (2013) Modulation of antioxidant machinery in α-tocopherol-enriched transgenic Brassica juncea plants tolerant to abiotic stress conditions. Protoplasma 250:1079–1089. https://doi.org/10.1007/s00709-013-0484-0
Kumar A, Kaachra A, Bhardwaj S, Kumar S (2014) Copper, zinc superoxide dismutase of Curcuma aromatica is a kinetically stable protein. Process Biochem 49:1288–1296. https://doi.org/10.1016/J.PROCBIO.2014.04.010
Kusunose E, Ichihara K, Noda Y, Kusunose M (1976) Superoxide dismutase from mycobacterium tuberculosis. J Biochem 80:1343–1352. https://doi.org/10.1093/oxfordjournals.jbchem.a131407
Lee Lee (2000) Chilling stress-induced changes of antioxidant enzymes in the leaves of cucumber: in gel enzyme activity assays. Plant Sci 159:75–85
Lee Y-P, Ahmad R, Lee H-S, Soo Swak S, Shafqat M, Kwon S-Y (2013) Improved tolerance of Cu/Zn superoxide dismutase and ascorbate peroxidase expressing transgenic tobacco seeds and seedlings against multiple abiotic stresses. Int J Agric Biol 15:725–730
Leonowicz G, Trzebuniak KF, Zimak-Piekarczyk P, Ślesak I, Mysliwa-Kurdziel B (2018) The activity of superoxide dismutases (SODs) at the early stages of wheat deetiolation. PLoS ONE 13:1–21. https://doi.org/10.1371/journal.pone.0194678
Lightfoot DJ, Mcgrann GRD, Able AJ (2017) The role of a cytosolic superoxide dismutase in barley-pathogen interactions. Mol Plant Pathol 18:323–335. https://doi.org/10.1111/mpp.12399
Lin Y-L, Lai Z-X (2013) Superoxide dismutase multigene family in longan somatic embryos: a comparison of CuZn-SOD, Fe-SOD, and Mn-SOD gene structure, splicing, phylogeny, and expression. Mol Breed 32:595–615. https://doi.org/10.1007/s11032-013-9892-2
Lin M-W, Lin M-T, Lin C-T (2002) Copper/zinc-superoxide dismutase from lemon cDNA and enzyme stability. J Agric Food Chem 50:7264–7270
Liu W, Yu K, He T, Li F, Zhang D, Liu J (2013) The low temperature induced physiological responses of Avena nuda L., a cold-tolerant plant species. Sci World J 658793. https://doi.org/10.1155/2013/658793
Liu Z, Holmes DJ, Faris JD, Chao S, Brueggeman RS, Edwards MC, Friesen TL (2015) Necrotrophic effector-triggered susceptibility (NETS) underlies the barley- Pyrenophora teres f. teres interaction specific to chromosome 6H. Mol Plant Pathol 16:188–200. https://doi.org/10.1111/mpp.12172
Lods LM, Dres C, Johnson C, Scholz DB, Brooks GJ (2000) The future of enzymes in cosmetics. Int J Cosmet Sci 22:85–94. https://doi.org/10.1046/j.1467-2494.2000.00012.x
Lomonte C, Sgherri C, Baker AJM, Kolev SD, Navari-Izzo F (2010) Antioxidative response of Atriplex codonocarpa to mercury. Environ Exp Bot 69:9–16. https://doi.org/10.1016/J.ENVEXPBOT.2010.02.012
Mahanty S, Kaul T, Pandey P, Reddy RA, Mallikarjuna G, Reddy CS, Sopory SK, Reddy MK (2012) Biochemical and molecular analyses of copper–zinc superoxide dismutase from a C4 plant Pennisetum glaucum reveals an adaptive role in response to oxidative stress. Gene 505:309–317. https://doi.org/10.1016/j.gene.2012.06.001
Maiti S, Ghosh N, Mandal C, Das K, Dey N, Adak MK (2012) Responses of the maize plant to chromium stress with reference to antioxidation activity. Brazilian J Plant Physiol 24:203–212. https://doi.org/10.1590/S1677-04202012000300007
Mann T, Keilin D (1938) Haemocuprein and hepatocuprein, copper-protein compounds of blood and liver in mammals. Proc R Soc London B Biol Sci 126
Manzanas García A, Carrizosa C, Vallejo Ocaña C, Samper Ots P, María Delgado Pérez J, Carretero Accame E, Gómez-Serranillos M, de la Morena del Valle L (2008) Superoxidase dismutase (SOD) topical use in oncologic patients: Treatment of acute cutaneous toxicity secondary to radiotherapy. Clin Transl Oncol 10:163–167. https://doi.org/10.1007/s12094-008-0174-0
McCord JM (1993) Human disease, free radicals, and the oxidant/antioxidant balance. Clin Biochem 26:351–357
McCord JM, Fridovich I (1969) Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 244:6049–6055 (1969)
Meloni DA, Oliva MA, Martinez CA, Cambraia J (2003) Photosynthesis and activity of superoxide dismutase, peroxidase and glutathione reductase in cotton under salt stress. Environ Exp Bot 49:69–76. https://doi.org/10.1016/S0098-8472(02)00058-8
Miller A-F (2012) Superoxide dismutases: Ancient enzymes and new insights. FEBS Lett 586:585–595. https://doi.org/10.1016/j.febslet.2011.10.048
Milone MT, Sgherri C, Clijsters H, Navari-Izzo F (2003) Antioxidative responses of wheat treated with realistic concentration of cadmium. Environ Exp Bot 50:265–276. https://doi.org/10.1016/S0098-8472(03)00037-6
Mittler R (2002) Oxidative stress, antioxidants and stress tolerance. Trends Plant Sci 7:405–410. https://doi.org/10.1016/S1360-1385(02)02312-9
Mittler R (2006) Abiotic stress, the field environment and stress combination. Trends Plant Sci 11:15–19. https://doi.org/10.1016/j.tplants.2005.11.002
Mittler R, Vanderauwera S, Gollery M, Van Breusegem F (2004) Reactive oxygen gene network of plants. Trends Plant Sci 9:490–498. https://doi.org/10.1016/j.tplants.2004.08.009
Molina-Rueda JJ, Tsai CJ, Kirby EG (2013) The Populus superoxide dismutase gene family and its responses to drought stress in transgenic poplar overexpressing a pine cytosolic glutamine synthetase (GS1a). PLoS ONE 8:e56421. https://doi.org/10.1371/journal.pone.0056421
Mutlu S, Karadağoğlu Ö, Atici Ö, Nalbantoğlu B (2013) Protective role of salicylic acid applied before cold stress on antioxidative system and protein patterns in barley apoplast. Biol Plant 57:507–513. https://doi.org/10.1007/s10535-013-0322-4
Ogawa K, Kanematsu S, Takabe K, Asada K (1995) Attachment of CuZn-superoxide dismutase to thylakoid membranes at the site of superoxide generation (PSI) in Spinach chloroplasts: detection by immuno-gold labeling after rapid freezing and substitution method. Plant Cell Physiol 36:565–573. https://doi.org/10.1093/oxfordjournals.pcp.a078795
Ogawa K, Kanematsu S, Asada K (1996) Intra- and extra-cellular localization of & cytosolic & CuZn-superoxide dismutase in spinach leaf and hypocotyl. Plant Cell Physiol 37:790–799. https://doi.org/10.1093/oxfordjournals.pcp.a029014
Panda SK (2007) Chromium-mediated oxidative stress and ultrastructural changes in root cells of developing rice seedlings. J Plant Physiol 164:1419–1428. https://doi.org/10.1016/j.jplph.2007.01.012
Park J, Ryu J, Jin LH, Bahn JH, Kim JA, Yoon CS, Kim DW, Han KH, Eum WS, Kwon HY, Kang T-C, Won MH, Kang JH, Cho S-W, Choi SY (2002) 9-polylysine protein transduction domain: enhanced penetration efficiency of superoxide dismutase into mammalian cells and skin. Mol Cells 13:202–208
Perry JJP, Shin DS, Getzoff ED, Tainer JA (2010) The structural biochemistry of the superoxide dismutases. Biochim Biophys Acta—Proteins Proteomics 1804:245–262. https://doi.org/10.1016/j.bbapap.2009.11.004
Puget K, Michelson AM (1974) Iron containing superoxide dismutases from luminous bacteria. Biochimie 56:1255–1267
Qiu-Fang Z, Yuan-Yuan L, Cai-Hong P, Cong-Ming L, Bao-Shan W (2005) NaCl enhances thylakoid-bound SOD activity in the leaves of C3 halophyte Suaeda salsa L. Plant Sci 168:423–430. https://doi.org/10.1016/J.PLANTSCI.2004.09.002
Qureshi MI, Abdin MZ, Qadir S, Iqbal M (2007) Lead-induced oxidative stress and metabolic alterations in Cassia angustifolia Vahl. Biol Plant 51:121–128. https://doi.org/10.1007/s10535-007-0024-x
Rai V, Vajpayee P, Singh SN, Mehrotra S (2004) Effect of chromium accumulation on photosynthetic pigments, oxidative stress defense system, nitrate reduction, proline level and eugenol content of Ocimum tenuiflorum L. Plant Sci 167:1159–1169. https://doi.org/10.1016/J.PLANTSCI.2004.06.016
Raja V, Majeed U, Kang H, Andrabi KI, John R (2017) Abiotic stress: interplay between ROS, hormones and MAPKs. Environ Exp Bot 137:142–157
Rani B (2009) High temperature induced changes in oxidative stress, antioxidant system and polypeptide pattern in Indian mustard [Brassica juncea (L.) Czern & Coss.]
Rasool S, Ahmad A, Siddiqi TO, Ahmad P (2013) Changes in growth, lipid peroxidation and some key antioxidant enzymes in chickpea genotypes under salt stress. Acta Physiol Plant 35:1039–1050. https://doi.org/10.1007/s11738-012-1142-4
Rivero RM, Ruiz JM, Garcı́a PC, López-Lefebre LR, Sánchez E, Romero L (2001) Resistance to cold and heat stress: accumulation of phenolic compounds in tomato and watermelon plants. Plant Sci 160:315–321. https://doi.org/10.1016/s0168-9452(00)00395-2
Robinett NG, Peterson RL, Culotta VC (2017) Eukaryotic Cu-only superoxide dismutases (SODs): a new class of SOD enzymes and SOD-like protein domains. J Biol Chem. https://doi.org/10.1074/jbc.TM117.000182
Rucińska R, Waplak S, Gwóźdź EA (1999) Free radical formation and activity of antioxidant enzymes in lupin roots exposed to lead. Plant Physiol Biochem 37:187–194. https://doi.org/10.1016/S0981-9428(99)80033-3
Russo M, Cocco S, Secondo A, Adornetto A, Bassi A, Nunziata A, Polichetti G, De Felice B, Damiano S, Serù R, Mondola P, Di Renzo G (2011) Cigarette smoke condensate causes a decrease of the gene expression of Cu–Zn superoxide dismutase, Mn superoxide dismutase, glutathione peroxidase, catalase, and free radical-induced cell injury in SH-SY5Y human neuroblastoma cells. Neurotox Res 19:49–54. https://doi.org/10.1007/s12640-009-9138-6
Sainz M, Díaz P, Monza J, Borsani O (2010) Heat stress results in loss of chloroplast Cu/Zn superoxide dismutase and increased damage to Photosystem II in combined drought-heat stressed Lotus japonicus. Physiol Plant 140:46–56. https://doi.org/10.1111/j.1399-3054.2010.01383.x
Salin ML, Bridges SM (1981) Absence of the iron-containing superoxide dismutase in mitochondria from mustard (Brassica campestris). Biochem J 195:229–233. https://doi.org/10.1042/bj1950229
Sandalio LM, Del Río LA (1987) Localization of superoxide dismutase in glyoxysomes from citrullus vulgaris. Functional Implications in Cellular Metabolism. J Plant Physiol 127:395–409. https://doi.org/10.1016/s0176-1617(87)80248-1
Scandalios JG (1993) Oxygen stress and superoxide dismutases. Plant Physiol 101:7–12. https://doi.org/10.1104/pp.101.1.7
Scandalios JG (2005) Oxidative stress: molecular perception and transduction of signals triggering antioxidant gene defenses. Brazilian J. Med. Biol. Res. 38:995–1014
Searcy KB, Searcy DG (1981) Superoxide dismutase from the archaebacterium thermoplasma acidophilum. Biochim Biophys Acta 670:39–46
Sen A, Alikamanoglu S (2013) Antioxidant enzyme activities, malondialdehyde, and total phenolic content of PEG-induced hyperhydric leaves in sugar beet tissue culture. Vitr Cell Dev Biol—Plant 49:396–404. https://doi.org/10.1007/s11627-013-9511-2
Shalata A, Mittova V, Volokita M, Guy M, Tal M (2001) Response of the cultivated tomato and its wild salt-tolerant relative Lycopersicon pennellii to salt-dependent oxidative stress: the root antioxidative system. Physiol Plant 112:487–494
Sharma P, Dubey RS (2005) Drought induces oxidative stress and enhances the activities of antioxidant enzymes in growing rice seedlings. Plant Growth Regul 46:209–221. https://doi.org/10.1007/s10725-005-0002-2
Sheng Y, Abreu IA, Cabelli DE, Maroney MJ, Miller A-F, Teixeira M, Valentine JS (2014) Superoxide dismutases and superoxide reductases. Chem Rev 114:3854–3918. https://doi.org/10.1021/cr4005296
Sheokand S, Kumari A, Sawhney V (2008) Effect of nitric oxide and putrescine on antioxidative responses under NaCl stress in chickpea plants. Physiol Mol Biol Plants 14:355–362. https://doi.org/10.1007/s12298-008-0034-y
Shetty NP, Mehrabi R, Lütken H, Haldrup A, Kema GHJ, Collinge DB, Jørgensen HJL (2007) Role of hydrogen peroxide during the interaction between the hemibiotrophic fungal pathogen Septoria tritici and wheat. New Phytol 174:637–647. https://doi.org/10.1111/j.1469-8137.2007.02026.x
Silva EN, Vieira SA, Ribeiro RV, Ponte LFA, Ferreira-Silva SL, Silveira JAG (2013) Contrasting physiological responses of jatropha curcas plants to single and combined stresses of salinity and heat. J Plant Growth Regul 32:159–169. https://doi.org/10.1007/s00344-012-9287-3
Sinha P, Khurana N, Nautiyal N (2012) Induction of oxidative stress and antioxidant enzymes by excess cobalt in mustard. J Plant Nutr 35:952–960. https://doi.org/10.1080/01904167.2012.663636
Song F, Yang C, Liu X, Li G (2006) Effect of salt stress on activity of superoxide dismutase (SOD) in Ulmus pumila L. J For Res 17:13–16. https://doi.org/10.1007/s11676-006-0003-7
Streller S, Wingsle G (1994) Pinus sylvestris L. needles contain extracellular CuZn superoxide dismutase. Planta 192:195–201. https://doi.org/10.1007/bf01089035
Subrahmanyam, D.: Effects of chromium toxicity on leaf photosynthetic characteristics and oxidative changes in wheat (Triticum aestivum L.). Photosynthetica. 46, 339–345 (2008). https://doi.org/10.1007/s11099-008-0062-4
Suzuki N, Mittler R (2006) Reactive oxygen species and temperature stresses: a delicate balance between signaling and destruction. Physiol Plant 126:45–51. https://doi.org/10.1111/j.0031-9317.2005.00582.x
Tamás L, Mistrík I, Huttová J, Halušková L, Valentovičová K, Zelinová V (2010) Role of reactive oxygen species-generating enzymes and hydrogen peroxide during cadmium, mercury and osmotic stresses in barley root tip. Planta 231:221–231. https://doi.org/10.1007/s00425-009-1042-z
Tepperman JM, Dunsmuir P (1990) Transformed plants with elevated levels of chloroplastic SOD are not more resistant to superoxide toxicity. Plant Mol Biol 14:501–511. https://doi.org/10.1007/BF00027496
Tertivanidis K, Goudoula C, Vasilikiotis C, Hassiotou E, Perl-Treves R, Tsaftaris A (2004) Superoxide dismutase transgenes in sugarbeets confer resistance to oxidative agents and the Fungus C. beticola. Transgenic Res 13:225–233. https://doi.org/10.1023/b:trag.0000034610.35724.04
Tuna AL, Kaya C, Dikilitas M, Higgs D (2008) The combined effects of gibberellic acid and salinity on some antioxidant enzyme activities, plant growth parameters and nutritional status in maize plants. Environ Exp Bot 62:1–9. https://doi.org/10.1016/j.envexpbot.2007.06.007
Tyagi S, Sharma S, Taneja M, Shumayla Kumar R, Sembi JK, Upadhyay SK (2017) Superoxide dismutases in bread wheat (Triticum aestivum L.): comprehensive characterization and expression analysis during development and, biotic and abiotic stresses. Agri Gene 6. https://doi.org/10.1016/j.aggene.2017.08.003
Upadhyaya H, Panda SK, Dutta BK (2008) Variation of physiological and antioxidative responses in tea cultivars subjected to elevated water stress followed by rehydration recovery. Acta Physiol Plant 30:457–468. https://doi.org/10.1007/s11738-008-0143-9
Verma S, Dubey RS (2003) Lead toxicity induces lipid peroxidation and alters the activities of antioxidant enzymes in growing rice plants. Plant Sci 164:645–655. https://doi.org/10.1016/S0168-9452(03)00022-0
Verma D, Lakhanpal N, Singh K (2019) Genome-wide identification and characterization of abiotic-stress responsive SOD (superoxide dismutase) gene family in Brassica juncea and B. rapa. BMC Genomics 20:227. https://doi.org/10.1186/s12864-019-5593-5
Viczián O, Künstler A, Hafez Y, Király L (2014) Catalases may play different roles in influencing resistance to virus-induced hypersensitive necrosis. Acta Phytopathol Entomol Hungarica 49:189–200. https://doi.org/10.1556/APhyt.49.2014.2.5
Vyas D, Kumar S (2005) Purification and partial characterization of a low temperature responsive Mn-SOD from tea (Camellia sinensis (L.) O. Kuntze). Biochem. Biophys Res Commun 329:831–838. https://doi.org/10.1016/j.bbrc.2005.02.051
Wang Y, Ying Y, Chen J, Wang X (2004) Transgenic Arabidopsis overexpressing Mn-SOD enhanced salt-tolerance. Plant Sci 167:671–677. https://doi.org/10.1016/J.PLANTSCI.2004.03.032
Wang F-Z, Wang Q-B, Kwon S-Y, Kwak S-S, Su W-A (2005) Enhanced drought tolerance of transgenic rice plants expressing a pea manganese superoxide dismutase. J Plant Physiol 162:465–472. https://doi.org/10.1016/j.jplph.2004.09.009
Wang W, Xia M, Chen J, Deng F, Yuan R, Zhang X, Shen F (2016) Genome-wide analysis of superoxide dismutase gene family in Gossypium raimondii and G. arboreum. Plant Gene 6:18–29. https://doi.org/10.1016/j.plgene.2016.02.002
Wang W, Zhang X, Deng F, Yuan R, Shen F (2017) Genome-wide characterization and expression analyses of superoxide dismutase (SOD) genes in Gossypium hirsutum. BMC Genom 18:376. https://doi.org/10.1186/s12864-017-3768-5
Xu S, Li Y, Hu J, Guan Y, Ma W, Zheng Y, Zhu S (2010) Responses of antioxidant enzymes to chilling stress in tobacco seedlings. Agric Sci China 9:1594–1601. https://doi.org/10.1016/S1671-2927(09)60256-X
Yogavel M, Mishra PC, Gill J, Bhardwaj PK, Dutt S, Kumar S, Ahuja PS, Sharma A (2008) Structure of a superoxide dismutase and implications for copper-ion chelation. Acta Crystallogr Sect D: Biol Crystallogr 64:892–901. https://doi.org/10.1107/S0907444908019069
Yost FJ, Fridovich I (1973) An iron-containing superoxide dismutase from Escherichia coli. J Biol Chem 248:4905–4908
Zhou Y, Hu L, Wu H, Jiang L, Liu S (2017) Genome-wide identification and transcriptional expression analysis of cucumber superoxide dismutase (SOD) family in response to various abiotic stresses. Int J Genomics 2017:1–14. https://doi.org/10.1155/2017/7243973
Zhu D, Scandalios JG (1993) Maize mitochondrial manganese superoxide dismutases are encoded by a differentially expressed multigene family. Proc Natl Acad Sci 90:9310–9314. https://doi.org/10.1073/pnas.90.20.9310
Zsigmond L, Szepesi Á, Tari I, Rigó G, Király A, Szabados L (2012) Overexpression of the mitochondrial PPR40 gene improves salt tolerance in Arabidopsis. Plant Sci 182:87–93. https://doi.org/10.1016/j.plantsci.2011.07.008
Acknowledgements
Authors are grateful to Panjab University, Chandigarh, India for research facilities. ST is grateful Science and Engineering Research Board (SERB), Government of India for financial support. We are also grateful to the Department of Science and Technology, Government of India for partial financial support under the Promotion of University Research and Scientific Excellence (PURSE) grant scheme.
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Tyagi, S., Shumayla, Singh, S.P., Upadhyay, S.K. (2019). Role of Superoxide Dismutases (SODs) in Stress Tolerance in Plants. In: Singh, S., Upadhyay, S., Pandey, A., Kumar, S. (eds) Molecular Approaches in Plant Biology and Environmental Challenges. Energy, Environment, and Sustainability. Springer, Singapore. https://doi.org/10.1007/978-981-15-0690-1_3
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