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      Hydrogen sulfide signaling in plant adaptations to adverse conditions: molecular mechanisms


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          This review focuses on recent advances relating to H 2S signaling mechanisms, and highlights interconnections between H 2S and H 2O 2 at the post-translational modification level and with ABA in stomatal movement.


          Hydrogen sulfide (H 2S) is a signaling molecule that regulates critical processes and allows plants to adapt to adverse conditions. The molecular mechanism underlying H 2S action relies on its chemical reactivity, and the most-well characterized mechanism is persulfidation, which involves the modification of protein thiol groups, resulting in the formation of persulfide groups. This modification causes a change of protein function, altering catalytic activity or intracellular location and inducing important physiological effects. H 2S cannot react directly with thiols but instead can react with oxidized cysteine residues; therefore, H 2O 2 signaling through sulfenylation is required for persulfidation. A comparative study performed in this review reveals 82% identity between sulfenylome and persulfidome. With regard to abscisic acid (ABA) signaling, widespread evidence shows an interconnection between H 2S and ABA in the plant response to environmental stress. Proteomic analyses have revealed persulfidation of several proteins involved in the ABA signaling network and have shown that persulfidation is triggered in response to ABA. In guard cells, a complex interaction of H 2S and ABA signaling has also been described, and the persulfidation of specific signaling components seems to be the underlying mechanism.

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          Most cited references82

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          Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family of START proteins.

          Type 2C protein phosphatases (PP2Cs) are vitally involved in abscisic acid (ABA) signaling. Here, we show that a synthetic growth inhibitor called pyrabactin functions as a selective ABA agonist. Pyrabactin acts through PYRABACTIN RESISTANCE 1 (PYR1), the founding member of a family of START proteins called PYR/PYLs, which are necessary for both pyrabactin and ABA signaling in vivo. We show that ABA binds to PYR1, which in turn binds to and inhibits PP2Cs. We conclude that PYR/PYLs are ABA receptors functioning at the apex of a negative regulatory pathway that controls ABA signaling by inhibiting PP2Cs. Our results illustrate the power of the chemical genetic approach for sidestepping genetic redundancy.
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            Regulators of PP2C phosphatase activity function as abscisic acid sensors.

            The plant hormone abscisic acid (ABA) acts as a developmental signal and as an integrator of environmental cues such as drought and cold. Key players in ABA signal transduction include the type 2C protein phosphatases (PP2Cs) ABI1 and ABI2, which act by negatively regulating ABA responses. In this study, we identify interactors of ABI1 and ABI2 which we have named regulatory components of ABA receptor (RCARs). In Arabidopsis, RCARs belong to a family with 14 members that share structural similarity with class 10 pathogen-related proteins. RCAR1 was shown to bind ABA, to mediate ABA-dependent inactivation of ABI1 or ABI2 in vitro, and to antagonize PP2C action in planta. Other RCARs also mediated ABA-dependent regulation of ABI1 and ABI2, consistent with a combinatorial assembly of receptor complexes.
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              H2S signals through protein S-sulfhydration.

              Hydrogen sulfide (H2S), a messenger molecule generated by cystathionine gamma-lyase, acts as a physiologic vasorelaxant. Mechanisms whereby H2S signals have been elusive. We now show that H2S physiologically modifies cysteines in a large number of proteins by S-sulfhydration. About 10 to 25% of many liver proteins, including actin, tubulin, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH), are sulfhydrated under physiological conditions. Sulfhydration augments GAPDH activity and enhances actin polymerization. Sulfhydration thus appears to be a physiologic posttranslational modification for proteins.

                Author and article information

                Role: Editor
                J Exp Bot
                J Exp Bot
                Journal of Experimental Botany
                Oxford University Press (UK )
                11 August 2021
                02 June 2021
                02 June 2021
                : 72
                : 16 , Special Issue: Plant Responses to Environmental Stress
                : 5893-5904
                [1 ]Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas and Universidad de Sevilla , Avenida Américo Vespucio, 49, 41092 Seville, Spain
                [2 ]Laboratory Center of Life Sciences, College of Life Sciences, Nanjing Agricultural University , Nanjing, PR China
                [3 ]VIB-Ugent , Belgium
                Author notes
                Author information
                © The Author(s) 2021. Published by Oxford University Press on behalf of the Society for Experimental Biology.

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

                : 21 February 2021
                : 19 May 2021
                : 24 May 2021
                : 05 July 2021
                Page count
                Pages: 12
                Funded by: Agencia Estatal de Investigación, DOI 10.13039/501100011033;
                Award ID: PID2019-109785GB-I00
                Award ID: RED2018-102397-T
                Funded by: Junta de Andalucía, DOI 10.13039/501100011011;
                Award ID: P18-RT-3154
                Award ID: US-1255781
                Funded by: Marie Skłodowska-Curie Grant Agreement;
                Award ID: 834120
                Funded by: National Natural Science Foundation of China, DOI 10.13039/501100001809;
                Award ID: 31607255
                Review Papers

                Plant science & Botany
                abscisic acid,persulfidation,proteomics,redox modifications,stomatal movement,sulfenylation


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