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      Plastoglobuli: Plastid Microcompartments with Integrated Functions in Metabolism, Plastid Developmental Transitions, and Environmental Adaptation

      1 , 2
      Annual Review of Plant Biology
      Annual Reviews

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          Abstract

          Plastoglobuli (PGs) are plastid lipoprotein particles surrounded by a membrane lipid monolayer. PGs contain small specialized proteomes and metabolomes. They are present in different plastid types (e.g., chloroplasts, chromoplasts, and elaioplasts) and are dynamic in size and shape in response to abiotic stress or developmental transitions. PGs in chromoplasts are highly enriched in carotenoid esters and enzymes involved in carotenoid metabolism. PGs in chloroplasts are associated with thylakoids and contain ∼30 core proteins (including six ABC1 kinases) as well as additional proteins recruited under specific conditions. Systems analysis has suggested that chloroplast PGs function in metabolism of prenyl lipids (e.g., tocopherols, plastoquinone, and phylloquinone); redox and photosynthetic regulation; plastid biogenesis; and senescence, including recycling of phytol, remobilization of thylakoid lipids, and metabolism of jasmonate. These functionalities contribute to chloroplast PGs' role in responses to stresses such as high light and nitrogen starvation. PGs are thus lipid microcompartments with multiple functions integrated into plastid metabolism, developmental transitions, and environmental adaptation. This review provides an in-depth overview of PG experimental observations, summarizes the present understanding of PG features and functions, and provides a conceptual framework for PG research and the realization of opportunities for crop improvement.

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          Most cited references149

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          Chlorophyll breakdown in higher plants.

          Chlorophyll breakdown is an important catabolic process of leaf senescence and fruit ripening. Structure elucidation of colorless linear tetrapyrroles as (final) breakdown products of chlorophyll was crucial for the recent delineation of a chlorophyll breakdown pathway which is highly conserved in land plants. Pheophorbide a oxygenase is the key enzyme responsible for opening of the chlorin macrocycle of pheophorbide a characteristic to all further breakdown products. Degradation of chlorophyll was rationalized by the need of a senescing cell to detoxify the potentially phototoxic pigment, yet recent investigations in leaves and fruits indicate that chlorophyll catabolites could have physiological roles. This review updates structural information of chlorophyll catabolites and the biochemical reactions involved in their formation, and discusses the significance of chlorophyll breakdown. This article is part of a Special Issue entitled: Regulation of Electron Transport in Chloroplasts. Copyright © 2010 Elsevier B.V. All rights reserved.
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            Pheophytin pheophorbide hydrolase (pheophytinase) is involved in chlorophyll breakdown during leaf senescence in Arabidopsis.

            During leaf senescence, chlorophyll is removed from thylakoid membranes and converted in a multistep pathway to colorless breakdown products that are stored in vacuoles. Dephytylation, an early step of this pathway, increases water solubility of the breakdown products. It is widely accepted that chlorophyll is converted into pheophorbide via chlorophyllide. However, chlorophyllase, which converts chlorophyll to chlorophyllide, was found not to be essential for dephytylation in Arabidopsis thaliana. Here, we identify pheophytinase (PPH), a chloroplast-located and senescence-induced hydrolase widely distributed in algae and land plants. In vitro, Arabidopsis PPH specifically dephytylates the Mg-free chlorophyll pigment, pheophytin (phein), yielding pheophorbide. An Arabidopsis mutant deficient in PPH (pph-1) is unable to degrade chlorophyll during senescence and therefore exhibits a stay-green phenotype. Furthermore, pph-1 accumulates phein during senescence. Therefore, PPH is an important component of the chlorophyll breakdown machinery of senescent leaves, and we propose that the sequence of early chlorophyll catabolic reactions be revised. Removal of Mg most likely precedes dephytylation, resulting in the following order of early breakdown intermediates: chlorophyll --> pheophytin --> pheophorbide. Chlorophyllide, the last precursor of chlorophyll biosynthesis, is most likely not an intermediate of breakdown. Thus, chlorophyll anabolic and catabolic reactions are metabolically separated.
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              Stay-green regulates chlorophyll and chlorophyll-binding protein degradation during senescence.

              Stay-green mutants are delayed in leaf senescence and have been identified from different plant species, including many crops. Functional stay-greens have the potential to increase plant productivity. In cosmetic stay-greens, however, retention of chlorophyll during senescence is uncoupled from a decline of photosynthetic capacity in these mutants. For many cosmetic stay-green mutants, including Gregor Mendel's famous green cotyledon pea variety, molecular defects were recently identified in orthologous stay-green genes. Stay-green genes encode members of a new family of chloroplast-located proteins, which are likely to function in dismantling of photosynthetic chlorophyll-apoprotein complexes. Their activity is considered as a prerequisite for both chlorophyll and apoprotein degradation during senescence.
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                Author and article information

                Journal
                Annual Review of Plant Biology
                Annu. Rev. Plant Biol.
                Annual Reviews
                1543-5008
                1545-2123
                April 28 2017
                April 28 2017
                : 68
                : 1
                : 253-289
                Affiliations
                [1 ]Plant Biology Section, School of Integrative Plant Science, Cornell University, Ithaca, New York 14853;
                [2 ]Laboratory of Plant Physiology, University of Neuchâtel, 2000 Neuchâtel, Switzerland;
                Article
                10.1146/annurev-arplant-043015-111737
                28125283
                e2584d19-be24-4ef6-b194-907f493932de
                © 2017
                History

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