**Stress-Induced Proteins in Recalcitrant Seeds During Deep Dormancy and Early Germination**

Marina I. Azarkovich

[77] Kitao M, Utsugi H, Kuramoto S, Tabuchi R, Fujimoto K, Lihpai S. Light-dependent photosynthetic characteristics indicated by chlorophyll fluorescence in five man‐ grove species native to Pohnpei Island, Micronesia. Physiol Plant 2003;117:376–82. [78] Fankhauser C, Chory J. Light control of plant development. Annu Rev Cell Dev Biol

[79] Sharma SS, Dietz KJ. The significance of amino acids and amino acid-derived mole‐ cules in plant responses and adaptation to heavy metal stress. J Exp Bot 2006;57:711–

[80] Yadav SK, Singla-Pareek SL, Sopory SK. An overview on the role of methylglyoxal

[81] Gong F, Hu X, Wang W. Proteomic analysis of crop plants under abiotic stress condi‐

[82] Kaur C, Ghosh A, Pareek A, Sopory SK, Singla-Pareek SL. Glyoxalases and stress tol‐

[83] Frolov A, Schmidt R, Spiller S, Greifenhagen U, Hoffmann R. Formation of argininederived advanced glycation end products in peptide-glucose mixtures during boil‐

[84] Bucala R, Tracey KJ, Cerami A. Advanced glycosylation products quench nitric oxide and mediate defective endothelium-dependent vasodilatation in experimental diabe‐

[85] Chevalier F, Chobert JM, Dalgalarrondo M, Choiset Y, Haertle T. Maillard glycation of beta-lactoglobulin induces conformation changes. Nahrung 2002;46:58–63.

[86] Brown LD, Cavalli C, Harwood JE, Casadei A, Teng CC, Traggiai C, Serra G, Bevilac‐ qua G, Battaglia FC. Plasma concentrations of carbohydrates and sugar alcohols in

[87] Henning C, Liehr K, Girndt M, Ulrich C, Glomb MA. Extending the spectrum of al‐

[88] Milkovska-Stamenova S, Schmidt R, Frolov A, Birkemeyer C. GC-MS method for the quantitation of carbohydrate intermediates in glycation systems. J Agric Food Chem

and glyoxalases in plants. Drug Metabol Drug Interact 2008;23:51–68.

tions: where to focus our research? Front Plant Sci 2015;6:418.

term newborns after milk feeding. Pediatr Res 2008;64:189–93.

pha-dicarbonyl compounds in vivo. J Biol Chem 2014;289:28676–88.

erance in plants. Biochem Soc Trans 2014;42:485–90.

ing. J Agric Food Chem 2014;62:3626–35.

316 Abiotic and Biotic Stress in Plants - Recent Advances and Future Perspectives

tes. J Clin Invest 1991;87:432–8.

2015;63:5911–9.

1997;13:203–29.

26.

Additional information is available at the end of the chapter

http://dx.doi.org/10.5772/61958

#### **Abstract**

The role and functions of dehydrins and heat shock proteins in seeds (especially in desic‐ cation-sensitive recalcitrant seeds) are discussed.

During the periods of dehydration, a wide variety of plants can express dehydration pro‐ teins (dehydrins), which are also members of the plant late embryogenesis abundant (LEA) protein family. Dehydrins have been most extensively studied in relation to drought and cold stresses. Dehydrins are synthesized in orthodox seeds, and their devel‐ opment at the final stage is associated with genetically determined seeds drying. Dehy‐ drins amount can reach 4% of total cell proteins. At the same time, dehydrins are found in desiccation-sensitive recalcitrant seeds. The following are the functions of dehydrins with experimental evidence: binding to water and ions, binding to phospholipids, radical scavenging, phosphorylation, binding to calcium, protection of enzymes, binding to cy‐ toskeletons, and binding to nucleic acids.

It seems evident that, in the embryo cells, heat shock induced changes in gene expression and HSP synthesis but did not result in translational discrimination of mRNAs for nonheat shock proteins. Such specific feature has been observed earlier for orthodox seeds during their development and early stages of germination. It is suggested that such re‐ sponse to HS is characteristic just of embryo tissues; it could be considered an additional molecular mechanism improving embryo tolerance to unfavorable environmental condi‐ tions.

**Keywords:** Recalcitrant seeds, temperature stress, dehydrins, heat shock proteins
