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      Alleviation of adverse effects of drought stress on wheat seed germination using atmospheric dielectric barrier discharge plasma treatment

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          Abstract

          Atmospheric dielectric barrier discharge (DBD) was attempted to improve the resistance of wheat seed to drought stress. Effects of DBD plasma on wheat seed germination, seedling growth, osmotic-adjustment products, lipid peroxidation, reactive oxygen species (ROS), antioxidant enzyme activity, abscisic acid, and drought resistant related genes expression under drought stress were investigated. The changes of the wheat seed coat before and after the DBD plasma treatment were explored. Experimental results showed that the DBD plasma treatment could alleviate the adverse effects of drought stress on wheat seed germination and seedling growth; the germination potential and germination rate increased by 27.2% and 27.6%, and the root length and shoot length of the wheat seedlings also increased. Proline and soluble sugar levels under drought stress were improved after the DBD plasma treatment, whereas the malondialdehyde content decreased. ROS contents under drought stress were reduced after the DBD plasma treatment, whereas the activities of superoxide dismutase, catalase, and peroxidase were promoted. DBD plasma treatment promoted abscisic acid generation in wheat seedlings, and it also regulated functional gene LEA1 and stimulated regulation genes SnRK2 and P5CS to resist drought stress. Etching effect and surface modification occurred on the seed coat after the DBD plasma treatment.

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          Rapid determination of free proline for water-stress studies

          Plant and Soil, 39(1), 205-207
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            The continuing conundrum of the LEA proteins.

            Research into late embryogenesis abundant (LEA) proteins has been ongoing for more than 20 years but, although there is a strong association of LEA proteins with abiotic stress tolerance particularly dehydration and cold stress, for most of that time, their function has been entirely obscure. After their initial discovery in plant seeds, three major groups (numbered 1, 2 and 3) of LEA proteins have been described in a range of different plants and plant tissues. Homologues of groups 1 and 3 proteins have also been found in bacteria and in certain invertebrates. In this review, we present some new data, survey the biochemistry, biophysics and bioinformatics of the LEA proteins and highlight several possible functions. These include roles as antioxidants and as membrane and protein stabilisers during water stress, either by direct interaction or by acting as molecular shields. Along with other hydrophilic proteins and compatible solutes, LEA proteins might also serve as "space fillers" to prevent cellular collapse at low water activities. This multifunctional capacity of the LEA proteins is probably attributable in part to their structural plasticity, as they are largely lacking in secondary structure in the fully hydrated state, but can become more folded during water stress and/or through association with membrane surfaces. The challenge now facing researchers investigating these enigmatic proteins is to make sense of the various in vitro defined functions in the living cell: Are the LEA proteins truly multi-talented, or are they still just misunderstood?
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              LEA proteins prevent protein aggregation due to water stress.

              LEA (late embryogenesis abundant) proteins in both plants and animals are associated with tolerance to water stress resulting from desiccation and cold shock. However, although various functions of LEA proteins have been proposed, their precise role has not been defined. Recent bioinformatics studies suggest that LEA proteins might behave as molecular chaperones, and the current study was undertaken to test this hypothesis. Recombinant forms of AavLEA1, a group 3 LEA protein from the anhydrobiotic nematode Aphelenchus avenae, and Em, a group 1 LEA protein from wheat, have been subjected to functional analysis. Heat-stress experiments with citrate synthase, which is susceptible to aggregation at high temperatures, suggest that LEA proteins do not behave as classical molecular chaperones, but they do exhibit a protective, synergistic effect in the presence of the so-called chemical chaperone, trehalose. In contrast, both LEA proteins can independently protect citrate synthase from aggregation due to desiccation and freezing, in keeping with a role in water-stress tolerance; similar results were obtained with lactate dehydrogenase. This is the first evidence of anti-aggregation activity of LEA proteins due to water stress. Again, a synergistic effect of LEA and trehalose was observed, which is significant given that non-reducing disaccharides are known to accumulate during dehydration in plants and nematodes. A model is proposed whereby LEA proteins might act as a novel form of molecular chaperone, or 'molecular shield', to help prevent the formation of damaging protein aggregates during water stress.
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                Author and article information

                Contributors
                wangtiecheng2008@126.com
                Journal
                Sci Rep
                Sci Rep
                Scientific Reports
                Nature Publishing Group UK (London )
                2045-2322
                30 November 2017
                30 November 2017
                2017
                : 7
                : 16680
                Affiliations
                [1 ]State Key Laboratory of Soil Erosion and Dryland Farming on the Loess Plateau, Institute of Soil and Water Conservation, Northwest A&F University, Shaanxi Province, 712100 P.R. China
                [2 ]ISNI 0000 0004 1760 4150, GRID grid.144022.1, College of Natural Resources and Environment, Northwest A&F University, ; Yangling, Shaanxi Province 712100 P.R. China
                [3 ]Key Laboratory of Plant Nutrition and the Agri-environment in Northwest China, Ministry of Agriculture, Yangling, Shaanxi 712100 P.R. China
                Article
                16944
                10.1038/s41598-017-16944-8
                5709406
                29192193
                976588d3-f4b4-4244-bd36-44cf4afe3fe1
                © The Author(s) 2017

                Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

                History
                : 9 August 2017
                : 19 November 2017
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