Oleosin expression and trafficking during oil body biogenesis in tobacco leaf cells

Wahlroos, Tony; Soukka, Jori; Denesyuk, Alexander I.; Wahlroos, Rina; Korpela, Timo; Kilby, Nigel J.

doi:10.1002/gene.10172

Cited by 45 publications

(39 citation statements)

References 34 publications

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“…No or few (authentic or simply background) oleosin transcripts are present in high-quality massively parallel signature sequencing or sequencing-by-synthesis leaf transcriptomes of Arabidopsis (Meyers et al, 2004) and rice (Nobuta et al, 2007). Regardless, oleosin encoded by an Arabidopsis gene transformed into tobacco (Nicotiana tabacum) leaf cells targets to lipid droplets via the ER (Wahlroos et al, 2003). In some species, the leaf lipid droplets may contain hydrophobic secondary metabolites (e.g.…”

Section: Discussionmentioning

confidence: 99%

Oil Bodies and Oleosins in Physcomitrella Possess Characteristics Representative of Early Trends in Evolution

Huang

Chung²,

Lin³

et al. 2009

Plant Physiology

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Searches of sequenced genomes of diverse organisms revealed that the moss Physcomitrella patens is the most primitive organism possessing oleosin genes. Microscopy examination of Physcomitrella revealed that oil bodies (OBs) were abundant in the photosynthetic vegetative gametophyte and the reproductive spore. Chromatography illustrated the neutral lipids in OBs isolated from the gametophyte to be largely steryl esters and triacylglycerols, and SDS-PAGE showed the major proteins to be oleosins. Reverse transcription-PCR revealed the expression of all three oleosin genes to be tissue specific. This tissue specificity was greatly altered via alternative splicing, a control mechanism of oleosin gene expression unknown in higher plants. During the production of sex organs at the tips of gametophyte branches, the number of OBs in the top gametophyte tissue decreased concomitant with increases in the number of peroxisomes and level of transcripts encoding the glyoxylate cycle enzymes; thus, the OBs are food reserves for gluconeogenesis. In spores during germination, peroxisomes adjacent to OBs, along with transcripts encoding the glyoxylate cycle enzymes, appeared; thus, the spore OBs are food reserves for gluconeogenesis and equivalent to seed OBs. The one-cell-layer gametophyte could be observed easily with confocal microscopy for the subcellular OBs and other structures. Transient expression of various gene constructs transformed into gametophyte cells revealed that all OBs were linked to the endoplasmic reticulum (ER), that oleosins were synthesized in extended regions of the ER, and that two different oleosins were colocated in all OBs.Eukaryotes and prokaryotes contain neutral lipids in subcellular droplets as food reserves and/or for other purposes (Hsieh and Huang, 2004;Martin and Parton, 2006;Goodman, 2008;Rajakumari et al., 2008). These lipid droplets are present in seeds, pollens, fruits, and flowers of higher plants; the vegetative and reproductive organs of lower plants, algae, fungi, and nematodes; mammalian organs/tissues, such as mammalian glands and adipose tissues; and bacteria. Among all these lipid droplets, oil bodies (OBs) in seeds are the most prominent and have been extensively studied.Seeds of diverse plant species store oils (triacylglycerols [TAGs]) as food reserves for germination and postgermination growth (Napier et al., 1996;Frandsen et al., 2001;Murphy, 2001;Hsieh and Huang, 2004).The TAGs are present in small subcellular, spherical OBs of approximately 0.5 to 2 mm in diameter. Each OB has a matrix of TAGs surrounded by a layer of phospholipids (PLs) and the structural protein oleosins. The massive oleosins completely cover the surface of the OBs and prevent them from coalescence; so, a large surface area per unit TAG is available for lipase binding and catalysis during germination. Each oleosin molecule has a characteristic long central hydrophobic stretch, which forms a hairpin penetrating into the matrix TAGs for stable anchorage.Other than being present in the seeds of plants, oleos...

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Section: Discussionmentioning

confidence: 99%

Oil Bodies and Oleosins in Physcomitrella Possess Characteristics Representative of Early Trends in Evolution

Huang

Chung²,

Lin³

et al. 2009

Plant Physiology

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“…All the available expression data (generated by us or available in expression databases) indicate that obap genes are predominantly expressed during embryo development, and their expression pattern is very similar to the oleosin genes. Fusions of OBAP1 to fluorescent protein tags demonstrate that OBAP1 colocalizes with OBs in tobacco leaf epidermal cells, which contains bona fide OBs (Wahlroos et al, 2003). These results were confirmed by immunolocalization experiments of OBAP1a in electron microscopy samples of mature rapeseed embryos.…”

Section: Discussionmentioning

confidence: 54%

The Evolutionary Conserved Oil Body Associated Protein OBAP1 Participates in the Regulation of Oil Body Size

et al. 2014

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A transcriptomic approach has been used to identify genes predominantly expressed in maize (Zea mays) scutellum during maturation. One of the identified genes is oil body associated protein1 (obap1), which is transcribed during seed maturation predominantly in the scutellum, and its expression decreases rapidly after germination. Proteins similar to OBAP1 are present in all plants, including primitive plants and mosses, and in some fungi and bacteria. In plants, obap genes are divided in two subfamilies. Arabidopsis (Arabidopsis thaliana) genome contains five genes coding for OBAP proteins. Arabidopsis OBAP1a protein is accumulated during seed maturation and disappears after germination. Agroinfiltration of tobacco (Nicotiana benthamiana) epidermal leaf cells with fusions of OBAP1 to yellow fluorescent protein and immunogold labeling of embryo transmission electron microscopy sections showed that OBAP1 protein is mainly localized in the surface of the oil bodies. OBAP1 protein was detected in the oil body cellular fraction of Arabidopsis embryos. Deletion analyses demonstrate that the most hydrophilic part of the protein is responsible for the oil body localization, which suggests an indirect interaction of OBAP1 with other proteins in the oil body surface. An Arabidopsis mutant with a transfer DNA inserted in the second exon of the obap1a gene and an RNA interference line against the same gene showed a decrease in the germination rate, a decrease in seed oil content, and changes in fatty acid composition, and their embryos have few, big, and irregular oil bodies compared with the wild type. Taken together, our findings suggest that OBAP1 protein is involved in the stability of oil bodies.

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“…Plants were illuminated using fluorescent lights (Lucalox®, type LU400/ HO/T/40) operated on a 16 hr day photoperiod. Mature, full-expanded, leaves were subjected to particle bombardment as described earlier [20].…”

Section: Plant Materials and Biolistic Gene Transfermentioning

confidence: 99%

“…Fluorescence from GFP and Nile Red were visualized using appropriate confocal microscope fluorescence filters as described earlier [20].…”

Section: Staining Of Oleosin-gfp Mutants Localized In Oil Bodies Withmentioning

confidence: 99%

“…The data suggested that interactions between adjacent oleosin proteins would give rise to a stable β-sheet structure that would extend around the surface of the seed oil bodies stabilizing them in emulsion systems [19]. We have demonstrated using GFP-fusions that rough endoplasmic reticulum (rER) is the site of oleosin biosynthesis and that oil bodies are laterally transported within the rER membranes [20]. Here it is presented that oleosins protect the oil bodies by preventing the oxidation and interaction of small molecules with oil bodies.…”

Section: Introductionmentioning

confidence: 99%

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Amino-Terminus of Oleosin Protein Defines the Size of Oil Bodies - Topological Model of Oleosin-Oil Body Complex

J¹,

P²

2015

Saha, J Plant Biochem Physiol

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Lipids formed in seeds of oilseed plant are stored in specific cytosolic structures called oil bodies, which are covered with oleosin proteins. Disruption of oleosin layer by heat treatment makes lipids susceptible to oxidation. By analyzing the amino acid sequence of Arabidopsis oleosin, unique domains were identified within the aminoterminus of the protein. Removal of these domains affected both the size of oil bodies and their susceptibility to lipid-specific stain, Nile Blue A. Amino-terminally truncated oleosin mutant, which was in fusion to green fluorescent protein (GFP), confined to rough endoplasmic reticulum (rER) suggesting that the amino-terminus of oleosin is required for the efficient lateral transportation of oleosin proteins from rER to oil bodies. The size of oil bodies covered by amino-terminal mutants was at least 5 times larger than native oil bodies. Based on the observations, a topological model was generated, which could explain how oleosin maintains and protects the integrity of oil bodies during seed storage. Citation: Wahlroos T, Soukka J, Denesyuk A, Susi P (2015) Amino-Terminus of Oleosin Protein Defines the Size of Oil Bodies -Topological Model of Oleosin-Oil Body Complex. J Plant Biochem Physiol 3: 155. Amino-Terminus of Oleosin

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Oleosin expression and trafficking during oil body biogenesis in tobacco leaf cells

Cited by 45 publications

References 34 publications

Oil Bodies and Oleosins in Physcomitrella Possess Characteristics Representative of Early Trends in Evolution

Oil Bodies and Oleosins in Physcomitrella Possess Characteristics Representative of Early Trends in Evolution

The Evolutionary Conserved Oil Body Associated Protein OBAP1 Participates in the Regulation of Oil Body Size

Amino-Terminus of Oleosin Protein Defines the Size of Oil Bodies - Topological Model of Oleosin-Oil Body Complex

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