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      Comparative Proteomics Analysis of the Root Apoplasts of Rice Seedlings in Response to Hydrogen Peroxide

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      PLoS ONE
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          Abstract

          Background

          Plant apoplast is the prime site for signal perception and defense response, and of great importance in responding to environmental stresses. Hydrogen peroxide (H 2O 2) plays a pivotal role in determining the responsiveness of cells to stress. However, how the apoplast proteome changes under oxidative condition is largely unknown. In this study, we initiated a comparative proteomic analysis to explore H 2O 2-responsive proteins in the apoplast of rice seedling roots.

          Methodology/Principal Findings

          14-day-old rice seedlings were treated with low concentrations (300 and 600 µM) of H 2O 2 for 6 h and the levels of relative electrolyte leakage, malondialdehyde and H 2O 2 were assayed in roots. The modified vacuum infiltration method was used to extract apoplast proteins of rice seedling roots, and then two-dimensional electrophoresis gel analysis revealed 58 differentially expressed protein spots under low H 2O 2 conditions. Of these, 54 were successfully identified by PMF or MS/MS as matches to 35 different proteins including known and novel H 2O 2-responsive proteins. Almost all of these identities (98%) were indeed apoplast proteins confirmed either by previous experiments or through publicly available prediction programs. These proteins identified are involved in a variety of processes, including redox homeostasis, cell wall modification, signal transduction, cell defense and carbohydrate metabolism, indicating a complex regulative network in the apoplast of seedling roots under H 2O 2 stress.

          Conclusions/Significance

          The present study is the first apoplast proteome investigation of plant seedlings in response to H 2O 2 and may be of paramount importance for the understanding of the plant network to environmental stresses. Based on the abundant changes in these proteins, together with their putative functions, we proposed a possible protein network that provides new insights into oxidative stress response in the rice root apoplast and clues for the further functional research of target proteins associated with H 2O 2 response.

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          Most cited references50

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          Galactinol and raffinose constitute a novel function to protect plants from oxidative damage.

          Galactinol synthase (GolS) is a key enzyme in the synthesis of raffinose family oligosaccharides that function as osmoprotectants in plant cells. In leaves of Arabidopsis (Arabidopsis thaliana) plants overexpressing heat shock transcription factor A2 (HsfA2), the transcription of GolS1, -2, and -4 and raffinose synthase 2 (RS2) was highly induced; thus, levels of galactinol and raffinose increased compared with those in wild-type plants under control growth conditions. In leaves of the wild-type plants, treatment with 50 mum methylviologen (MV) increased the transcript levels of not only HsfA2, but also GolS1, -2, -3, -4, and -8 and RS2, -4, -5, and -6, the total activities of GolS isoenzymes, and the levels of galactinol and raffinose. GolS1- or GolS2-overexpressing Arabidopsis plants (Ox-GolS1-11, Ox-GolS2-8, and Ox-GolS2-29) had increased levels of galactinol and raffinose in the leaves compared with wild-type plants under control growth conditions. High intracellular levels of galactinol and raffinose in the transgenic plants were correlated with increased tolerance to MV treatment and salinity or chilling stress. Galactinol and raffinose effectively protected salicylate from attack by hydroxyl radicals in vitro. These findings suggest the possibility that galactinol and raffinose scavenge hydroxyl radicals as a novel function to protect plant cells from oxidative damage caused by MV treatment, salinity, or chilling.
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            Important roles of drought- and cold-inducible genes for galactinol synthase in stress tolerance in Arabidopsis thaliana.

            Raffinose family oligosaccharides (RFO) accumulating during seed development are thought to play a role in the desiccation tolerance of seeds. However, the functions of RFO in desiccation tolerance have not been elucidated. Here we examine the functions of RFO in Arabidopsis thaliana plants under drought- and cold-stress conditions, based on the analyses of function and expression of genes involved in RFO biosynthesis. Sugar analysis showed that drought-, high salinity- and cold-treated Arabidopsis plants accumulate a large amount of raffinose and galactinol, but not stachyose. Raffinose and galactinol were not detected in unstressed plants. This suggests that raffinose and galactinol are involved in tolerance to drought, high salinity and cold stresses. Galactinol synthase (GolS) catalyses the first step in the biosynthesis of RFO from UDP-galactose. We identified three stress-responsive GolS genes (AtGolS1, 2 and 3) among seven Arabidopsis GolS genes. AtGolS1 and 2 were induced by drought and high-salinity stresses, but not by cold stress. By contrast, AtGolS3 was induced by cold stress but not by drought or salt stress. All the GST fusion proteins of GST-AtGolS1, 2 and 3 expressed in Escherichia coli had galactinol synthase activities. Overexpression of AtGolS2 in transgenic Arabidopsis caused an increase in endogenous galactinol and raffinose, and showed reduced transpiration from leaves to improve drought tolerance. These results show that stress-inducible galactinol synthase plays a key role in the accumulation of galactinol and raffinose under abiotic stress conditions, and that galactinol and raffinose may function as osmoprotectants in drought-stress tolerance of plants.
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              Pectin methylesterases: cell wall enzymes with important roles in plant physiology.

              Pectin methylesterases catalyse the demethylesterification of cell wall polygalacturonans. In dicot plants, these ubiquitous cell wall enzymes are involved in important developmental processes including cellular adhesion and stem elongation. Here, I highlight recent studies that challenge the accepted views of the mechanism and function of pectin methylesterases, including the co-secretion of pectins and pectin methylesterases into the apoplasm, new action patterns of mature pectin methylesterases and a possible function of the pro regions of pectin methylesterases as intramolecular chaperones.
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                Author and article information

                Contributors
                Role: Editor
                Journal
                PLoS One
                plos
                plosone
                PLoS ONE
                Public Library of Science (San Francisco, USA )
                1932-6203
                2011
                10 February 2011
                : 6
                : 2
                : e16723
                Affiliations
                [1]Laboratory of Molecular Biology and MOE Laboratory of Protein Science, School of Life Sciences, Tsinghua University, Beijing, People's Republic of China
                Instituto de Biología Moleculary Celular de Plantas, Spain
                Author notes

                Conceived and designed the experiments: JYL LZ. Performed the experiments: LZ SAB. Analyzed the data: LZ. Contributed reagents/materials/analysis tools: LZ. Wrote the paper: JYL LZ CJD.

                Article
                PONE-D-10-03899
                10.1371/journal.pone.0016723
                3037377
                21347307
                b9087078-f33e-4ab1-a7b1-082872e7f07b
                Zhou et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
                History
                : 25 October 2010
                : 22 December 2010
                Page count
                Pages: 11
                Categories
                Research Article
                Biology
                Biochemistry
                Proteins
                Defense Proteins
                Proteome
                Regulatory Proteins
                Genomics
                Functional Genomics
                Genome Expression Analysis
                Plant Science
                Plants
                Seedlings
                Plant Physiology
                Proteomics
                Protein Abundance
                Spectrometric Identification of Proteins

                Uncategorized
                Uncategorized

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