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      Comparison of full-length and conserved segments of wheat dehydrin DHN-5 overexpressed in Arabidopsis thaliana showed different responses to abiotic and biotic stress

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      Functional Plant Biology
      CSIRO Publishing

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          Abstract

          Dehydrins (DHNs) are among the most common proteins accumulated in plants under water-related stress. They typically contain at least three conserved sequences designated as the Y-, S- and K-segments. The present work aims to highlight the role of the K-segments in plant tolerance to biotic and abiotic stresses. For this purpose, transgenic Arabidopsis thaliana (L.) Heyhn. lines expressing distinct wheat (Triticum aestivum L.) DHN-5 truncated constructs with or without the K-segments were generated. Our results showed that unlike the derivative lacking a K-segment, constructs containing only one or two K-segments enhanced the tolerance of A. thaliana to diverse stresses and were similar to the full-length wheat DHN-5. Moreover, compared with the wild-type and the YS form, the transgenic plants overexpressing wheat DHN-5 with K-segments maintained higher superoxide dismutase, catalase and peroxide dismutase enzymatic activity, and accumulated lower levels of H2O2 and malondialdehyde. In addition, we demonstrated that lines like A. thaliana overexpressing wheat DHN-5 showed increased resistance to fungal infections caused by Botrytis cinerea and Alternaria solani. Finally, the overexpression of the different forms of wheat DHN-5 led to the regulation of the expression of several genes involved in the jasmonic acid signalling pathway.

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          Most cited references32

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          Plant dehydrins and stress tolerance: versatile proteins for complex mechanisms.

          Dehydrins (DHNs), or group 2 LEA (Late Embryogenesis Abundant) proteins, play a fundamental role in plant response and adaptation to abiotic stresses. They accumulate typically in maturing seeds or are induced in vegetative tissues following salinity, dehydration, cold, and freezing stress. The generally accepted classification of dehydrins is based on their structural features, such as the presence of conserved sequences, designated as Y, S, and K segments. The K segment representing a highly conserved 15 amino acid motif forming amphiphilic α-helix is especially important since it has been found in all dehydrins. Since more than 20 years, they are thought to play an important protective role during cellular dehydration but their precise function remains unclear. This review outlines the current status of the progress made towards the structural, physico-chemical and functional characterization of plant dehydrins and how these features could be exploited in improving stress tolerance in plants. 
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            Dehydrins: A commonalty in the response of plants to dehydration and low temperature

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              Plant dehydrins — Tissue location, structure and function

              Dehydrins (DHNs) are part of a large group of highly hydrophilic proteins known as LEA (Late Embryogenesis Abundant). They were originally identified as group II of the LEA proteins. The distinctive feature of all DHNs is a conserved, lysine-rich 15-amino acid domain, EKKGIMDKIKEKLPG, named the K-segment. It is usually present near the C-terminus. Other typical dehydrin features are: a track of Ser residues (the S-segment); a consensus motif, T/VDEYGNP (the Y-segment), located near the N-terminus; and less conserved regions, usually rich in polar amino acids (the Φ-segments). They do not display a well-defined secondary structure. The number and order of the Y-, S-and K-segments define different DHN sub-classes: YnSKn, YnKn, SKn, Kn and KnS. Dehydrins are distributed in a wide range of organisms including the higher plants, algae, yeast and cyanobacteria. They accumulate late in embryogenesis, and in nearly all the vegetative tissues during normal growth conditions and in response to stress leading to cellular dehydration (e.g. drought, low temperature and salinity). DHNs are localized in different cell compartments, such as the cytosol, nucleus, mitochondria, vacuole, and the vicinity of the plasma membrane; however, they are primarily localized to the cytoplasm and nucleus. The precise function of dehydrins has not been established yet, but in vitro experiments revealed that some DHNs (YSKn-type) bind to lipid vesicles that contain acidic phospholipids, and others (KnS) were shown to bind metals and have the ability to scavenge hydroxyl radicals [Asghar, R. et al. Protoplasma 177 (1994) 87–94], protect lipid membranes against peroxidation or display cryoprotective activity towards freezing-sensitive enzymes. The SKn-and K-type seem to be directly involved in cold acclimation processes. The main question arising from the in vitro findings is whether each DHN structural type could possess a specific function and tissue distribution. Much recent in vitro data clearly indicates that dehydrins belonging to different subclasses exhibit distinct functions.
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                Author and article information

                Journal
                Functional Plant Biology
                Functional Plant Biol.
                CSIRO Publishing
                1445-4408
                2016
                2016
                : 43
                : 11
                : 1048
                Article
                10.1071/FP16134
                f836f809-c69a-47eb-a0ed-b5893ba1b153
                © 2016
                History

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