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      Integration of the Physiology, Transcriptome and Proteome Reveals the Molecular Mechanism of Drought Tolerance in Cupressus gigantea

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      Forests
      MDPI AG

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          Abstract

          Drought stress can dramatically impair woody plant growth and restrict the geographical distribution of many tree species. To better understand the dynamics between the response and mechanism of Cupressus gigantea to drought and post-drought recovery, a comparative analysis was performed, relying on physiological measurements, RNA sequencing (RNA-Seq) and two-dimensional gel electrophoresis (2-DE) proteins. In this study, the analyses revealed that photosynthesis was seriously inhibited, while osmolyte contents, antioxidant enzyme activity and non-enzymatic antioxidant contents were all increased under drought stress in seedlings. Re-watering led to a recovery in most of the parameters analyzed, mainly the photosynthetic parameters and osmolyte contents. Transcriptomic and proteomic profiling suggested that most of the differentially expressed genes (DEGs) and differentially expressed proteins (DEPs) were specifically altered, and a few were consistently altered. Drought induced a common reduction in the level of DEGs and DEPs associated with photosynthesis. Notably, DEGs and DEPs involved in reactive oxygen species (ROS) scavenging, such as ascorbate oxidase and superoxide dismutase (SOD), showed an inverse pattern under desiccation. This study may improve our understanding of the underlying molecular mechanisms of drought resistance in C. gigantea and paves the way for more detailed molecular analysis of the candidate genes.

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          Most cited references54

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          Abiotic Stress Signaling and Responses in Plants.

          As sessile organisms, plants must cope with abiotic stress such as soil salinity, drought, and extreme temperatures. Core stress-signaling pathways involve protein kinases related to the yeast SNF1 and mammalian AMPK, suggesting that stress signaling in plants evolved from energy sensing. Stress signaling regulates proteins critical for ion and water transport and for metabolic and gene-expression reprogramming to bring about ionic and water homeostasis and cellular stability under stress conditions. Understanding stress signaling and responses will increase our ability to improve stress resistance in crops to achieve agricultural sustainability and food security for a growing world population.
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            Superoxide dismutases: I. Occurrence in higher plants.

            Shoots, roots, and seeds of corn (Zea mays L., cv. Michigan 500), oats (Avena sativa L., cv. Au Sable), and peas (Pisum sativum L., cv. Wando) were analyzed for their superoxide dismutase content using a photochemical assay system consisting of methionine, riboflavin, and p-nitro blue tetrazolium. The enzyme is present in the shoots, roots, and seeds of the three species. On a dry weight basis, shoots contain more enzyme than roots. In seeds, the enzyme is present in both the embryo and the storage tissue. Electrophoresis indicated a total of 10 distinct forms of the enzyme. Corn contained seven of these forms and oats three. Peas contained one of the corn and two of the oat enzymes. Nine of the enzyme activities were eliminated with cyanide treatment suggesting that they may be cupro-zinc enzymes, whereas one was cyanide-resistant and may be a manganese enzyme. Some of the leaf superoxide dismutases were found primarily in mitochondria or chloroplasts. Peroxidases at high concentrations interfere with the assay. In test tube assays of crude extracts from seedlings, the interference was negligible. On gels, however, peroxidases may account for two of the 10 superoxide dismutase forms.
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              Structure of spinach photosystem II-LHCII supercomplex at 3.2 Å resolution.

              During photosynthesis, the plant photosystem II core complex receives excitation energy from the peripheral light-harvesting complex II (LHCII). The pathways along which excitation energy is transferred between them, and their assembly mechanisms, remain to be deciphered through high-resolution structural studies. Here we report the structure of a 1.1-megadalton spinach photosystem II-LHCII supercomplex solved at 3.2 Å resolution through single-particle cryo-electron microscopy. The structure reveals a homodimeric supramolecular system in which each monomer contains 25 protein subunits, 105 chlorophylls, 28 carotenoids and other cofactors. Three extrinsic subunits (PsbO, PsbP and PsbQ), which are essential for optimal oxygen-evolving activity of photosystem II, form a triangular crown that shields the Mn4CaO5-binding domains of CP43 and D1. One major trimeric and two minor monomeric LHCIIs associate with each core-complex monomer, and the antenna-core interactions are reinforced by three small intrinsic subunits (PsbW, PsbH and PsbZ). By analysing the closely connected interfacial chlorophylls, we have obtained detailed insights into the energy-transfer pathways between the antenna and core complexes.

                Author and article information

                Contributors
                Journal
                Forests
                Forests
                MDPI AG
                1999-4907
                March 2022
                March 01 2022
                : 13
                : 3
                : 401
                Article
                10.3390/f13030401
                4cc20672-804d-48fa-a16d-8f7d83c4b54f
                © 2022

                https://creativecommons.org/licenses/by/4.0/

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