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      Roles and maturation of iron–sulfur proteins in plastids

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          Abstract

          One reason why iron is an essential element for most organisms is its presence in prosthetic groups such as hemes or iron–sulfur (Fe–S) clusters, which are notably required for electron transfer reactions. As an organelle with an intense metabolism in plants, chloroplast relies on many Fe–S proteins. This includes those present in the electron transfer chain which will be, in fact, essential for most other metabolic processes occurring in chloroplasts, e.g., carbon fixation, nitrogen and sulfur assimilation, pigment, amino acid, and vitamin biosynthetic pathways to cite only a few examples. The maturation of these Fe–S proteins requires a complex and specific machinery named SUF (sulfur mobilisation). The assembly process can be split in two major steps, (1) the de novo assembly on scaffold proteins which requires ATP, iron and sulfur atoms, electrons, and thus the concerted action of several proteins forming early acting assembly complexes, and (2) the transfer of the preformed Fe–S cluster to client proteins using a set of late-acting maturation factors. Similar machineries, having in common these basic principles, are present in the cytosol and in mitochondria. This review focuses on the currently known molecular details concerning the assembly and roles of Fe–S proteins in plastids.

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          Acyl-lipid metabolism.

          Acyl lipids in Arabidopsis and all other plants have a myriad of diverse functions. These include providing the core diffusion barrier of the membranes that separates cells and subcellular organelles. This function alone involves more than 10 membrane lipid classes, including the phospholipids, galactolipids, and sphingolipids, and within each class the variations in acyl chain composition expand the number of structures to several hundred possible molecular species. Acyl lipids in the form of triacylglycerol account for 35% of the weight of Arabidopsis seeds and represent their major form of carbon and energy storage. A layer of cutin and cuticular waxes that restricts the loss of water and provides protection from invasions by pathogens and other stresses covers the entire aerial surface of Arabidopsis. Similar functions are provided by suberin and its associated waxes that are localized in roots, seed coats, and abscission zones and are produced in response to wounding. This chapter focuses on the metabolic pathways that are associated with the biosynthesis and degradation of the acyl lipids mentioned above. These pathways, enzymes, and genes are also presented in detail in an associated website (ARALIP: http://aralip.plantbiology.msu.edu/). Protocols and methods used for analysis of Arabidopsis lipids are provided. Finally, a detailed summary of the composition of Arabidopsis lipids is provided in three figures and 15 tables.
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            Network analysis of the MVA and MEP pathways for isoprenoid synthesis.

            Isoprenoid biosynthesis is essential for all living organisms, and isoprenoids are also of industrial and agricultural interest. All isoprenoids are derived from prenyl diphosphate (prenyl-PP) precursors. Unlike isoprenoid biosynthesis in other living organisms, prenyl-PP, as the precursor of all isoprenoids in plants, is synthesized by two independent pathways: the mevalonate (MVA) pathway in the cytoplasm and the 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway in plastids. This review focuses on progress in our understanding of how the precursors for isoprenoid biosynthesis are synthesized in the two subcellular compartments, how the underlying pathway gene networks are organized and regulated, and how network perturbations impact each pathway and plant development. Because of the wealth of data on isoprenoid biosynthesis, we emphasize research in Arabidopsis thaliana and compare the synthesis of isoprenoid precursor molecules in this model plant with their synthesis in other prokaryotic and eukaryotic organisms.
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              Sulfur assimilation in photosynthetic organisms: molecular functions and regulations of transporters and assimilatory enzymes.

              Sulfur is required for growth of all organisms and is present in a wide variety of metabolites having distinctive biological functions. Sulfur is cycled in ecosystems in nature where conversion of sulfate to organic sulfur compounds is primarily dependent on sulfate uptake and reduction pathways in photosynthetic organisms and microorganisms. In vascular plant species, transport proteins and enzymes in this pathway are functionally diversified to have distinct biochemical properties in specific cellular and subcellular compartments. Recent findings indicate regulatory processes of sulfate transport and metabolism are tightly connected through several modes of transcriptional and posttranscriptional mechanisms. This review provides up-to-date knowledge in functions and regulations of sulfur assimilation in plants and algae, focusing on sulfate transport systems and metabolic pathways for sulfate reduction and synthesis of downstream metabolites with diverse biological functions.
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                Author and article information

                Contributors
                ++ 33 3 72 74 51 57 , nicolas.rouhier@univ-lorraine.fr
                Journal
                J Biol Inorg Chem
                J. Biol. Inorg. Chem
                Journal of Biological Inorganic Chemistry
                Springer Berlin Heidelberg (Berlin/Heidelberg )
                0949-8257
                1432-1327
                18 January 2018
                18 January 2018
                2018
                : 23
                : 4
                : 545-566
                Affiliations
                [1 ]ISNI 0000 0001 2194 6418, GRID grid.29172.3f, Université de Lorraine, Interactions Arbres-Microorganismes, UMR1136, ; 54500 Vandoeuvre-lès-Nancy, France
                [2 ]ISNI 0000 0004 0445 8430, GRID grid.461861.c, Biochimie et Physiologie Moléculaire des Plantes, CNRS/INRA/Université Montpellier 2, ; SupAgro Campus, 34060 Montpellier, France
                Article
                1532
                10.1007/s00775-018-1532-1
                6006212
                29349662
                1303e913-860e-4ba6-8a03-99f7e4fbf16a
                © The Author(s) 2018, corrected publication May/2018

                Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License ( http://creativecommons.org/licenses/by/4.0/), which permits use, duplication, 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.

                History
                : 18 October 2017
                : 14 December 2017
                Funding
                Funded by: FundRef 10.13039/501100001665, Agence Nationale de la Recherche;
                Award ID: ANR-2013-BSV6-0002-01
                Categories
                Minireview
                Custom metadata
                © SBIC 2018

                Inorganic & Bioinorganic chemistry
                biogenesis,iron–sulfur proteins,plastids,electron transfer,photosynthesis

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