The role of plastoglobules in thylakoid lipid remodeling during plant development

Rottet, Sarah; Besagni, Céline; Kessler, Félix

doi:10.1016/j.bbabio.2015.02.002

Cited by 144 publications

(108 citation statements)

References 145 publications

(201 reference statements)

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“…In both chloro- and chromoplasts, CCD4 is one of the major components of plastoglobuli proteomes [137,140], indicating a role for this enzyme in the regulation of carotenoid metabolism in plastid types with marked differences in functionality and carotenoid composition [142]. Moreover, CCD4 protein level is strongly reduced in Arabidopsis mutants defective in the ABC1K1 and ABC1K3 plastoglobuli kinases, suggesting phosphorylation as a post-transcriptional modification necessary for CCD4 protein stability and supporting main activity and localization in plastoglobuli [143].…”

Section: Plant Ccdsmentioning

confidence: 99%

Carotenoid Cleavage Oxygenases from Microbes and Photosynthetic Organisms: Features and Functions

Ahrazem

Gómez-Gómez

Rodrigo

et al. 2016

IJMS

143

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Apocarotenoids are carotenoid-derived compounds widespread in all major taxonomic groups, where they play important roles in different physiological processes. In addition, apocarotenoids include compounds with high economic value in food and cosmetics industries. Apocarotenoid biosynthesis starts with the action of carotenoid cleavage dioxygenases (CCDs), a family of non-heme iron enzymes that catalyze the oxidative cleavage of carbon–carbon double bonds in carotenoid backbones through a similar molecular mechanism, generating aldehyde or ketone groups in the cleaving ends. From the identification of the first CCD enzyme in plants, an increasing number of CCDs have been identified in many other species, including microorganisms, proving to be a ubiquitously distributed and evolutionarily conserved enzymatic family. This review focuses on CCDs from plants, algae, fungi, and bacteria, describing recent progress in their functions and regulatory mechanisms in relation to the different roles played by the apocarotenoids in these organisms.

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Section: Plant Ccdsmentioning

confidence: 99%

Carotenoid Cleavage Oxygenases from Microbes and Photosynthetic Organisms: Features and Functions

Ahrazem

Gómez-Gómez

Rodrigo

et al. 2016

IJMS

143

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“…PG were first thought only to be lipid storage sites. But a series of studies revealed that PG actively participate in lipid synthesis and repair (Eugeni Piller et al, 2012; Rottet et al, 2015; Spicher and Kessler, 2015). It was shown that PG contain enzymes such as tocopherol cyclase (VTE1), NAD(P)H dehydrogenase C1 (NDC1), and phytyl ester synthase (PES), as well as others (Zbierzak et al, 2010; Eugeni Piller et al, 2011, 2014; Lippold et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

Identification of Plastoglobules as a Site of Carotenoid Cleavage

et al. 2016

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Carotenoids play an essential role in light harvesting and protection from excess light. During chloroplast senescence carotenoids are released from their binding proteins and are eventually metabolized. Carotenoid cleavage dioxygenase 4 (CCD4) is involved in carotenoid breakdown in senescing leaf and desiccating seed, and is part of the proteome of plastoglobules (PG), which are thylakoid-associated lipid droplets. Here, we demonstrate that CCD4 is functionally active in PG. Leaves of Arabidopsis thaliana ccd4 mutants constitutively expressing CCD4 fused to yellow fluorescent protein showed strong fluorescence in PG and reduced carotenoid levels upon dark-induced senescence. Lipidome-wide analysis indicated that β-carotene, lutein, and violaxanthin were the principle substrates of CCD4 in vivo and were cleaved in senescing chloroplasts. Moreover, carotenoids were shown to accumulate in PG of ccd4 mutant plants during senescence, indicating translocation of carotenoids to PG prior to degradation.

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“…The current study revealed that α-, β-, γ-, and δ-tocopherol homologs were also present in leaves and stems. Leaves and stems contain chloroplasts, where lipidcontaining thylakoid membranes are found [18][19][20]. This may explain the high levels of lipid-soluble α-tocopherol homologs that are present in leaves and stems.…”

Section: Discussionmentioning

confidence: 95%

Distribution of Eight Vitamin E Homologs Found in 81 Plants Using LC-MS3

Inoue¹,

Honma²,

Otsuka³

et al. 2017

J Nutr Food Sci

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To the best of our knowledge, this is the first study to use liquid chromatography/multistage mass spectrometry to demonstrate the distribution of eight vitamin E homologs in plants. Many tocopherol homologs, which showed higher antioxidant activity than tocotrienol homologs, were discovered and α-tocopherol, which had the highest antioxidant activity among these homologs, was widely distributed in all plants. In addition, α-tocopherol occurred at high concentrations in the leaves of plants belonging to the sumac family, which is native to tropical regions. Furthermore, 25.9% of plants contained α-tocopherol alone, whereas the remaining 74.1% contained α-tocopherol in combination with other homologs. The detection frequency was the highest for a combination of α-tocopherol and γ-tocopherol, which is a precursor of α-tocopherol in plants. The highest number of vitamin E homologs was found in leaves, followed by stems, flowers, branches, and buds. Furthermore, tocotrienol homologs were present only in leaves. This indicates that the distribution of homologs in plants reflects the intensity of the antioxidant activity of homologs. It also suggests that the distribution of α-tocopherol in combination with γ-tocopherol is influenced by the α-tocopherol synthetic pathway in plants.

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The role of plastoglobules in thylakoid lipid remodeling during plant development

Cited by 144 publications

References 145 publications

Carotenoid Cleavage Oxygenases from Microbes and Photosynthetic Organisms: Features and Functions

Carotenoid Cleavage Oxygenases from Microbes and Photosynthetic Organisms: Features and Functions

Identification of Plastoglobules as a Site of Carotenoid Cleavage

Distribution of Eight Vitamin E Homologs Found in 81 Plants Using LC-MS3

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