A Brassica napus Lipase Locates at the Membrane Contact Sites Involved in Chloroplast Development

Tan, Xiao‐Li; Wang, Qiuye; Tian, Baoxia; Zhang, Henan; Lu, Daoli; Zhou, Jia

doi:10.1371/journal.pone.0026831

Cited by 34 publications

(44 citation statements)

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“…BnCLIP1 enzyme exhibited a discrete localization on the outer envelope membrane at the junction between the ER and plastids. The subcellular distribution of a protein such as BnCLIP1 at the PLAM is consistent with a potential role of these sites in the coordinated synthesis of lipids between the ER and plastids (Tan et al, 2011). Yet, it is unknown whether proteins of this kind have only a biosynthetic role at the PLAMs, such as lipid synthesis and transport, or have a scaffolding role to tether the two organelles together.…”

Section: The Er Is a Pleomorphic Organelle Whose Morphology And Dynamsupporting

confidence: 64%

“…The applied force of 400 pN, which is a magnitude compatible with proteinprotein interactions, could not drag a chloroplast free from its attached ER (Andersson et al, 2007). Using confocal imaging of a fluorescent fusion, the Brassica napus CLIP1 lipase/acylhydrolase (BnCLIP1) has been detected recently in transient expression in tobacco (Nicotiana tabacum) at the ER-chloroplast contact sites (Tan et al, 2011), also known as PLAMs. BnCLIP1 enzyme exhibited a discrete localization on the outer envelope membrane at the junction between the ER and plastids.…”

Section: The Er Is a Pleomorphic Organelle Whose Morphology And Dynammentioning

confidence: 99%

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Advances in Plant ER Architecture and Dynamics

Stefano

Brandizzí

2017

Plant Physiol.

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Section: The Er Is a Pleomorphic Organelle Whose Morphology And Dynamsupporting

confidence: 64%

Section: The Er Is a Pleomorphic Organelle Whose Morphology And Dynammentioning

confidence: 99%

Advances in Plant ER Architecture and Dynamics

Stefano

Brandizzí

2017

Plant Physiol.

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“…In agreement with this idea is the finding that wild-type plants in which MES16 was targeted to the chloroplast and consequently demethylated FCCs before export from the organelle and exposure to CYP89A9, exhibited a cyp89a9 mutant-like phenotype (i.e., abundance of NCCs was substantially increased) ( Figure 7). There is increasing evidence in the literature that chloroplasts and the ER are associated through defined membrane contact sites (Andersson et al, 2007;Tan et al, 2011). Such contact sites have been shown to have an important function for lipid transfer between chloroplast and the ER and might involve protein-protein interaction between the partaking membranes.…”

Section: Discussionmentioning

confidence: 99%

Cytochrome P450 CYP89A9 Is Involved in the Formation of Major Chlorophyll Catabolites during Leaf Senescence in Arabidopsis

et al. 2013

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Nonfluorescent chlorophyll catabolites (NCCs) were described as products of chlorophyll breakdown in Arabidopsis thaliana. NCCs are formyloxobilin-type catabolites derived from chlorophyll by oxygenolytic opening of the chlorin macrocycle. These linear tetrapyrroles are generated from their fluorescent chlorophyll catabolite (FCC) precursors by a nonenzymatic isomerization inside the vacuole of senescing cells. Here, we identified a group of distinct dioxobilin-type chlorophyll catabolites (DCCs) as the major breakdown products in wild-type Arabidopsis, representing more than 90% of the chlorophyll of green leaves. The molecular constitution of the most abundant nonfluorescent DCC (NDCC), At-NDCC-1, was determined. We further identified cytochrome P450 monooxygenase CYP89A9 as being responsible for NDCC accumulation in wild-type Arabidopsis; cyp89a9 mutants that are deficient in CYP89A9 function were devoid of NDCCs but accumulated proportionally higher amounts of NCCs. CYP89A9 localized outside the chloroplasts, implying that FCCs occurring in the cytosol might be its natural substrate. Using recombinant CYP89A9, we confirm FCC specificity and show that fluorescent DCCs are the products of the CYP89A9 reaction. Fluorescent DCCs, formed by this enzyme, isomerize to the respective NDCCs in weakly acidic medium, as found in vacuoles. We conclude that CYP89A9 is involved in the formation of dioxobilin-type catabolites of chlorophyll in Arabidopsis.

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“…Related hypotheses discussed in the field for both ER to chloroplast envelope and interenvelope transport involve plastid‐associated membranes (PLAMs) and hemifusion. PLAMs involve stable membrane contact between the ER and the chloroplast and have been observed by microscopy and optical manipulation . While information on PLAMs is still scarce, they are likely similar to mitochondria‐associated membranes (MAMs), which have been extensively studied and reviewed .…”

Section: Er To Chloroplast Envelope and Interenvelope Transportmentioning

confidence: 99%

Lipid Trafficking in Plant Cells

Hurlock

Roston

Wang

et al. 2014

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Plant cells contain unique organelles such as chloroplasts with an extensive photosynthetic membrane. In addition, specialized epidermal cells produce an extracellular cuticle composed primarily of lipids, and storage cells accumulate large amounts of storage lipids. As lipid assembly is associated only with discrete membranes or organelles, there is a need for extensive lipid trafficking within plant cells, more so in specialized cells and sometimes also in response to changing environmental condi- Plant cells have many membranes that are generally comparable to those in animal cells including the plasma, mitochondrial, nuclear and peroxisomal membranes. In addition, plant cells contain unique membrane-bound compartments such as the chloroplast, vacuole and symbiosome (1) and have other unique cellular structures composed of lipids, e.g. the cuticle of epidermal cells. As the key photosynthetic organelle in plants, one focus of plant lipid research has been on the chloroplast. It is surrounded by the outer and the inner envelope membranes and encompasses one of the most extensive membrane systems found in nature, the photosynthetic membrane organized into thylakoids. This membrane is unique in its lipid composition with the two galactolipids, monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG), being predominant (2,3). Unlike animal cells that synthesize fatty acids (FAs) in the cytoplasm and assemble glycerolipids primarily in the endoplasmic reticulum (ER), Golgi apparatus and mitochondria (4), plant cells synthesize FAs in the stroma of the chloroplast and assemble glycerolipids mainly by two pathways, the prokaryotic/plastid pathway in the chloroplast envelope membranes and the eukaryotic pathway in the ER (5), aside from lipid assembly or modification in mitochondria and Golgi. It should be noted that while lipid metabolism occurs in plastids other than chloroplasts, for example, chromoplasts in fruits and flowers or leucoplasts in storage tissues, most research on lipid trafficking has focused on chloroplasts. The origin of specific glycerolipids from either the ER or the chloroplast pathways in plants can be determined owing to the specificity of the respective acyltransferases (6,7). The ER-localized acyltransferase preferentially transfers 18 carbon FAs to the sn-2 (carbon 2) position of the glycerol backbone, whereas the chloroplast-localized acyltransferase preferentially transfers 16 carbon FAs to the sn-2 position of the glycerol backbone (6,7). Because of this difference in enzyme specificity, it has been well established that plants use both chloroplast-and ER-derived lipids as precursors in the assembly of chloroplast-specific galactolipids (7-9).www.traffic.dk 915

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A Brassica napus Lipase Locates at the Membrane Contact Sites Involved in Chloroplast Development

Cited by 34 publications

References 58 publications

Advances in Plant ER Architecture and Dynamics

Advances in Plant ER Architecture and Dynamics

Cytochrome P450 CYP89A9 Is Involved in the Formation of Major Chlorophyll Catabolites during Leaf Senescence in Arabidopsis

Lipid Trafficking in Plant Cells

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