Document Type : Review Article
Author
Young researchers club, Boroujed branch, Islamic Azad University, Boroujerd, Iran
Abstract
Seed storage proteins are synthesized as sources of carbon, nitrogen and sulfur for the next generation of plants. Reactive oxygen species serve as second messengers for signal transduction; however, molecular targets of oxidant signaling have not been defined. Here, many researchers showes that ligand–receptor mediated signaling promotes reactive oxygen species– dependent protein carbonylation. Carbonylation of the majority of proteins occurred transiently. Protein carbonylation in response to ligand–receptor interactions represents a novel mechanism in redox signaling. The role of protein oxidation in dormancy alleviation could be discussed in relation to the nature of the carbonylated proteins. Carbonylation of storage proteins has previously been reported in dry mature Arabidopsis seeds, and it was suggested that carbonylation of these proteins facilitates their mobilization during germination. Also, in sunflower seeds, breaking of dormancy in the dry state may be associated with preparation for storage protein mobilization. Hence, ROS accumulation appears to be a key signal governing cell activity during after-ripening. The role of specific proteins in maintenance of seed viability or longevity has been well documented However, quality and hardiness in seeds determined by protein contrnt
Keywords
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Job, C., Rajjou, L., Lovigny, Y., Belghazi, M. and Job, D. (2005) Patterns of protein oxidation in Arabidopsis seeds and during germination. Plant Physiol. 138, 790–802.
Johansson, E., Olsson, O. and Nystro¨m, T. (2004) Progression and specificity of protein oxidation in the life cycle of Arabidopsis thaliana. J. Biol. Chem. 279, 22204–22208.
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Cabiscol, E., Piulats, E., Echave, P., Herrero, E. and Ros, J. (2000) Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae. J. Biol. Chem. 275, 27393–27398.
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Stadtman ER and Levine RL. Protein oxidation. Ann NY Acad Sci 899: 191–208, 2000. Levine RL. Carbonyl modified proteins in cellular regulation, aging, and disease. Free Radic Biol Med 32: 790–796, 2002.
. Krystyna Oracz, Hayat El-Maarouf Bouteau, Jill M. Farrant, Keren Cooper, Maya Belghazi, Claudette Job, Dominique Job, Franc¸oise Corbineau and Christophe Bailly. 2007. ROS production and protein oxidation as a novel mechanism for seed dormancy alleviation. The Plant Journal. 10. 1-14.
Grimsrud PA, Xie H, Griffin TJ, and Bernlohr DA. Oxidative stress and covalent modification of protein with bioactive aldehydes. J Biol Chem 283: 21837–21841, 2008.
Sayre LM, Lin D, Yuan Q, Zhu X, and Tang X. Protein adducts generated from products of lipid oxidation: focus on HNE and one. Drug Metab Rev 38: 651–675, 2006.
Stadtman ER and Levine RL. Chemical modification of proteins by reactive oxygen species. In: Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases, edited by Dalle–Donne I, Scaloni A, and Butterfield DA. Hoboken NJ: John Wiley & Sons, 2006, pp. 3–23.
Burcham, P.C. and Kuhan, Y.T. (1996) Introduction of Carbonyl groups into proteins by the lipid peroxidation product, malondialdehyde. Biochem. Biophys. Res. Commun 220,996–1001.
Corbineau F, Bagniol S, Coˆme D (1990) Sunflower (Helianthus annuus) seed dormancy and its regulation by ethylene. Isr J Bot 39: 313–325
Kwak JM, Nguyen V, Schoeder JI (2006) The role of reactive oxygen species in hormonal responses. Plant Physiol 141: 323–329
Finkelstein R, ReevesW, Ariizumi T, Steber C (2008) Molecular aspects of seed dormancy. Annu Rev Plant Biol 59: 387–415
Oracz K, El-Maarouf-Bouteau H, Bogatek R, Corbineau F, Bailly C (2008) Release of sunflower seed dormancy by cyanide: cross-talk with ethylene signalling pathway. J Exp Bot 59: 2241–2251
Dalle-Donne, I., Giustarini, D., Colombo, R., Rossi, R. and Milzani, A. (2003) Protein carbonylation in human diseases. Trends Mol. Med. 9, 169–176.
Ding, Q., Dimayuga, E. and Keller, J.N. (2006) Proteasome regulation of oxidative stress in aging and age-related diseases of the CNS. Antioxid. Redox Signal. 8, 163–172.
Nystro¨m, T. (2005) Role of oxidative carbonylation in protein quality control and senescence. EMBO J. 24, 1311–1317.
Job, C., Rajjou, L., Lovigny, Y., Belghazi, M. and Job, D. (2005) Patterns of protein oxidation in Arabidopsis seeds and during germination. Plant Physiol. 138, 790–802.
Liu, W. and Wang, J.Y. (2005) Modification of protein by polyunsaturated fatty acid ester peroxidation products. Biochim. Biophys. Acta. 1752, 93–98.
Tabe, L., Hagan, N. and Higgins, T.J. (2002) Plasticity of seed protein composition in response to nitrogen and sulfur availability. Curr. Opin. Plant Biol. 5, 212–217.
Preston K.R. (1998). Protein-carbohydrate interactions. In: Hamer R.J. and Hoseney R.C. (eds), Interactions: The Keys to Cereal Quality, St. Paul, MN: AACCI, pp. 83_91.
Finney K.F., Yamazaki W.T., Youngs V.L. and Rubenthaler G.L. (1987). Quality of hard, soft and durum
wheats. In: Geyne E.G. (ed.), Wheat and Wheat Improvement, 2nd edn. Medison, WI: Agronomy Monograph No. 13, pp. 667_748.
Gaines C.S., Finney P.F., Fleege L.M. and Andrews L.C. (1996). Predicting a hardness measurement using the single-kernel characterization system. Cereal Chemistry 73: 278_283.
Osborne B.G., Turnbull K.M., Anderssen R.S., Rahman S., Sharp P.J. and Appels R. (2001). The hardness locus of Australian wheat lines. Australian Journal of Agricultural Research 52: 1275_1286.
Kosmolak F.G. (1978). Grinding time-A screening test for kernel hardness in wheat. Canadian Journal of Plant Science 58: 415_420.
Kramer H.H. and Albrecht H.R. (1948). The adaptation to small samples of the pearling test for kernel hardness in wheat. Journal of the American Society of Agronomy 20: 422_431.
Manely M., McGill A.E.J. and Osborne B.G. (1996). Whole wheat grain hardness measurement by near infrared spectroscopy. In: Davis A.M.C. and Williams P. (eds), Near Infrared Spectroscopy: The Future Waves. Chichester, UK: NIR Publications, pp. 466_470.
Wanjugi H.W., Hogg A.C., Martin J.M. and Giroux M.J. (2007). The role of puroindoline A and B individually and in combination on grain hardness and starch association. Crop Science 47: 67_76.
Dubreil L., Compoint J.P. and Marion D. (1997). Interaction of puroindolines with wheat flour polar lipids determines their foaming properties. Journal of Agricultural and Food Chemistry 45: 108_116.
Giroux M.J. and Morris C.F. (1998). Wheat grain hardness results from highly conserved mutations in the friabilin components puroindoline a and b. The Proceedings of the National Academy of Sciences, USA 95: 6262_6266.
Turnbull K.M. and Rahman S. (2002). Endosperm texture in wheat. Journal of Cereal Science 36:327_337.
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