M. K. NADA, A.M. ABDELHALIM, H.FAHHAD, A.2020-02-032020-02-032009Abba, S., S. Ghignone and P. Bonfante (2006). A dehydration-inducible gene in the truffle Tuber borchii identifies a novel group of Dehydrins. BMC Genomics Research article, 7: 39-54. Allagulova, C. R., F. R. Gimalov, F. M. Shakirova and S. Abba (2006). The plant Dehydrins: structure and putative functions. Biochemistry – Moscow, 68: 945-951. Altschul, S. F., T. L. Madden, A. A. Schaffer, J. H. Zhang, Z. Zhang, W. Miller and D. J. Lipman (1997). Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Research, 25: 3389-3402. Blackman, S. A., R. L. Obendorf and A. C. Leopold (1995). Desiccation tolerance in developing soybean seeds: the role of stress proteins. Physiol. Plant, 93: 630-638. Chen, Y., J. S. Burris (1990). Role of carbohydrates in desiccation tolerance and membrane behavior in maturing maize seeds. Crop Sci., 30: 971-975. Chung, E., S. Y. Kim, Y. S. Yi, and D. Choi (2003). Capsicum annuum Dehydrin, an Osmotic-Stress Gene in Hot Pepper Plants. Mol. Cells, 15(3):327-332 Close, T. J. (1996). Dehydrins: emergence of a biochemical role of a family of plant dehydration proteins. Physiol. Plant, 97: 795-803. Close, T. J. (1997). Dehydrins: a commonality in the response of plants to dehydration and low temperature. Physiol. Plant, 100: 291-296. Close, T. J., R. D. Fenton and F. Moonan (1993). A view of plant Dehydrins using antibodies specific to the carboxy terminal peptide. Plant Mol. Biol., 23: 279-286. Diab, A. A., A. Ageez, B. A. Abdelgawad and T. Z. Salem (2007). Cloning, sequence analysis and in silico mapping of a drought-inducible gene coding for sadenosylmethionine decarboxylase from durum wheat. World Applied Sciences Journal, 2: 333-340. Dure, L. I. (1993). Structural motifs in LEA proteins of higher plants. Response of Plants to Cellular Dehydration during Environmental Stress. American Society of Plant Physiologists, Rockville, MD, p 91-103. Godoy, J. A., R. Lunar, S. TorresSchumann, J. Moreno, M. Rodrigo and J. A. Pintor-Toro (1994). Expression, tissue distribution and subcellular localization of Dehydrin TAS14 in salt-stressed tomato plants. Plant Mol. Biol., 26: 1921- 1934. Grosselindemann, E., M. obertson, J. A. Wilmer, and P. M. Chandler (1998) Genetic variation in pea (Pisum) Dehydrins: sequence elements responsible for length differences between Dehydrin alleles and between Dehydrin loci in Pisum sativum L. Theor. Appl. Genet., 96: 1186-1192. Hundertmark, M. and D. K. Hincha (2008). LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana. BMC Genomics Research article ,9: 1-22. Ingram, J. and D. Bartels (1996). The molecular basis of dehydration tolerance in plants. Annu Rev. Plant Physiol. Plant Mol. Biol., 47: 377- 403. Koag, M. C., R. D. Fenton, S. Wilkens and T. J. Close (2003). The binding of maize DHN1 to lipid vesicles: gain of structure and lipid specificity. Plant Physiology, 131: 309- 316. Koster, K. L. and A. C. Leopold (1988). Sugars and desiccation tolerance in seeds. Plant Physiol., 88: 829-832. Li, R., S. H. Brawley and T. J. Close (1998). Proteins immunologically related to Dehydrins in fucoud algae. J. Phycol., 34: 642-650. Muthalif, M. M. and L. J. Rowland (1994). ldentification of DehydrinLike Proteins Responsive to Chilling in Floral Buds of Blueberry (Vaccinium, section Cyanococcus). Plant Physiol., 104: 1439-1447. O’Rourke, E. J., C. Chevalier, S. Boiteux, A. Labigne, L. Ielpi and J. P. Radicella (2000). A novel 3- methyladenine DNA glycosylase from Helicobacter pylori defines a new class within the endonuclease III family of base excision repair glycosylases. J. Biol. Chem., 275: 20077-20083. Rinne, P. L. H., P. L. M. Kaikuranta, L. H. W. van der Plas and C. van der Schoot (1999). Dehydrins in coldacclimated apices of birch (Betula pubescens Ehrh.): production, localization and potential role in rescuing enzyme function during dehydration. Planta, 209: 377-388. Roberton, M. and P. M. Chandler (1992). Pea Dehydrins: identification, characterization and expression. Plant Mol. Biol., 19: 1031-1044. Saitou, N. and M. Nei (1987). The neighborjoining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol., 4: 406-425. Sambrook, J.; E. F. Fritsch, and T. Maniatis, (1989). Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. Skriver, K., J. Mundy (1990). Gene expression in response to abscisic acid and osmotic stress. The Plant Cell, 2: 503-512. Soulages, J. L., K. Kim, E. L. Arrese, C. Walters and J. C. Cushman (2003). Conformation of a group 2 late embryogenesis abundant protein from soybean: evidence of poly (Lproline)-type II structure. Plant Physiol., 131: 963-975. Thomashow, M. F. (1999). Plant cold acclimation: Freezing tolerance genes and regulatory mechanisms. Ann. Rev. Plant Physiol., 50: 571-599. Thompson, J. D., D. G. Higgins and T. J. Gibson (1994). CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22: 4673-4680. Wise, M. J. and A. Tunnacliffe (2004). POPP the question: what do LEA proteins do?. Plant Sci., 9: 13-17.https://t.ly/AZ3ZkMSA Google ScholarThroughout their life cycle, plants are subjected to many adverse environmental stresses such as drought, high temperatures, etc. that dramatically affect plant survival and reduce productivity. To cope with such stresses, plants produce several stress-induced proteins that play a definite role in protecting plants during such severe conditions (Muthalif and Rowland, 1994). The late embryonic stage represents one of the abiotic stress conditions where the seed starts to lose water content during desiccation. Several molecules have been found to play vital roles in seed development and are thought to help in saving the embryos during desiccation. These include sugars (Koster and Leopold, 1988; Chen and Burris, 1990) and proteins, among which are the lateembryogenesis abundant proteins (LEA) (Blackman et al., 1995; Dure, 1993; Close, 1996; Ingram and Bartels, 1996). LEA proteins were found in the seeds of several plants and in vegetative organs, especially under abiotic stress conditions (Thomashow, 1999; Hundertmark and Hincha, 2008). According to amino acid sequence homology, LEA proteins have been separated into different groups (Hundertmark and Hincha, 2008). From these groups the LEA D11 family (LEA type 2 proteins), also known as Dehydrins (Close, 1997), have been estimated to comprise up to 4% of the total seed protein. (Wise and Tunnacliffe, 2004). Expression of the Dehydrin proteins have been found to be associated with the protection of various types of plant cells from osmotic stresses, such as those caused by desiccation, salt, and low temperatures (Skriver and Mundy, 1990; Close, 1996; Ingram and Bartels, 1996; Allagulova et al., 2006). Hyper-osmotic conditions and low temperatures cause cellular dehydration, resulting in the reduction of cytosolic volumes and the alteration of cellular mechanisms. Toward survival, plants accumulate Dehydrin proteins during these conditions in the dehydrating plant tissue, (Abba et al., 2006). Several studies revealed that Dehydrins are widely distributed in the plant kingdom (Abba et al., 2006), in brown algae (Li et al., 1998), in lichen Selaginella lepidophylla (Close, 1997) and in cyanobacterium (Close et al., 1993). A number of Dehydrin proteins have been isolated and studied; the physiochemical and/or structural mechaenCLONINGDEHYDRIN GENESHALOPHYTESArticle