Nucleotide sequence of an Arabidopsis thaliana oleosin gene

Rooijen, Gijs J. H. van; Terning, Linda I.; Moloney, Maurice M.

doi:10.1007/bf00047721

Cited by 44 publications

(35 citation statements)

References 14 publications

(17 reference statements)

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“…This domain is composed entirely of hydrophobic or non-polar amino acid residues and is assumed to insert into the lipid milieu of the oil body. The hydrophobic central domain of the B. napus oleosin Bnlll has recently been demonstrated to have an unusual p-strand structure (Li et a/., 1992) which confirms secondary structure prediction data for all seed oleosins (Murphy, 1990;Murphy eta/., 1991). The N-and C-terminal domains of oleosins are much less conserved at the sequence level, but generally exhibit polar characteristics.…”

Section: Introductionsupporting

confidence: 66%

“…structure Each of the putative pollen oleosin protein sequences was subjected to secondary structure prediction analysis as performed previously with the seed oleosins (Li et a/., 1992). The results demonstrate that the hydrophobic domains, extending from residues 18-79 of 13 and residues 12-90 of C98, are strongly predicted to have a p-strand structure with no turns (data not shown).…”

Section: F G L T G L S S L S W V L S Y F R Q ---A S Q R V P D Q I E Lmentioning

confidence: 99%

“…Furthermore, their similarity to the embryo-expressed oleosins is extended to secondary structure characteristics, especially the linear hydrophobic P-strand, implying conservation of the features necessary for association with lipids. It may be significant that cloned B. napus and A. thaliana oleosin genes (Keddie et a/., 1992a;van Rooijen et a/., 1992) contain an intron which separates the exons encoding the hydrophobic central domain and the variable C-terminal domain. One might thus envisage a process of exon shuffling which has resulted in the lack of conservation of oleosin C-termini.…”

Section: Evolution Of Gametophytic and Sporophytic Oleosinsmentioning

confidence: 99%

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Characterization of a new class of oleosins suggests a male gametophyte specific lipid storage pathway

et al. 1993

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SummaryThe expression and sequences of two related antherspecific cDNAs (13 and C98) of Brassica napus (oilseed rape) were examined. These cDNAs were found to exhibit significant predicted amino acid sequence similarity with a group of seed-specific proteins, the oleosins, which are involved in oil body membrane structure. Pollen of 6. napus also contains oil bodies, and the synthesis and accumulation of these organelles correlates with expression of the 1 3 and C98 transcripts. The protein content of purified pollen oil bodies was or absence of possible oleosins. One major protein species of 14 kDa was identified and subjected t o N-terminal amino acid sequence determination. The sequence of this pollen oil body associated protein is homologous to the predicted sequence of one of the anther-specific cDNAs, 13, implying that this cDNA represents an anther-specific oleosin gene expressed in developing pollen. The expression of other genes active during seed oil body formation was also examined, and these were found to be specific t o the sporophyte, inferring the existence of specific components of the pathway of lipid synthesis and storage in the male gametophyte. These possibilities and the relationship between different oleosin genes are discussed. therefore examined in order to determine the presence

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Section: Introductionsupporting

confidence: 66%

Section: F G L T G L S S L S W V L S Y F R Q ---A S Q R V P D Q I E Lmentioning

confidence: 99%

Section: Evolution Of Gametophytic and Sporophytic Oleosinsmentioning

confidence: 99%

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Characterization of a new class of oleosins suggests a male gametophyte specific lipid storage pathway

et al. 1993

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“…The amount of oleosins is high, especially in Brassica seeds accounting for 8% of the total seed proteins. With the molecular weight of about 15 to 26 kDa, oleosins are often specifically abundant in seeds, and inducible by factors such as water, abscisic acid, jasmonate acid and sorbitol (Vance & Huang, 1988;Hatzopoulos et al 1990;Qu & Huang, 1990;van Rooijen et al 1992). Additionally, several oleosin isomers form a family in one species, with distinct expression characters.…”

Section: Plant Oil Bodies and Oleosinsmentioning

confidence: 99%

“…Presently many oleosins and their genes have been isolated from Arabidopsis thaliana, rapeseed, sunflower, carrot, maize, soybean and cotton (Hatzopoulos et al 1990;Qu & Huang 1990;Cummins & Murphy 1992;Huang 1992;Keddie & Edwards 1992;van Rooijen et al 1992;Hughes et al 1993). Concerning the gene structures, oleosin genes in maize, soybean, and pine do not contain introns, whereas those from Brassicaceae have one intron.…”

mentioning

confidence: 99%

Oleosin fusion expression systems for the production of recombinant proteins

Ling

2007

Biologia

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For the production of recombinant proteins, product purification is potentially difficult and expensive. Plant oleosins are capable of anchoring onto the surface of natural or artificial oil bodies. The oleosin fusion expression systems allow products to be extracted with oil bodies. In vivo, oleosin fusions are produced and directly localized to natural oil bodies in transgenic plant seeds. Via the oleosin fusion technology the thrombin inhibitor hirudin has been successfully produced and commercially used in Canada. In vitro, artificial oil bodies have been used as "carriers" for the recombinant proteins expressed in transformed microbes. In this article, plant oleosins, strategies and limitations of the oleosin fusion expression systems are summarized, alongside with progress and applications. The oleosin fusion expression systems reveal an available way to produce recombinant biopharmaceuticals at large scale.

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

Wahlroos

Soukka

Denesyuk

et al. 2003

Genesis

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We have established a versatile method for studying the interaction of the oleosin gene product with oil bodies during oil body biogenesis in plants. Our approach has been to transiently express a green fluorescent protein (GFP)-tagged Arabidopsis oleosin gene fusion in tobacco leaf cells containing bona fide oil bodies and then to monitor oleosin-GFP expression using real-time confocal laser scanning microscopy. We show that normally non-oil-storing tobacco leaf cells are able to synthesize and then transport oleosin-GFP fusion protein to leaf oil bodies. Synthesis and transport of oleosin-GFP fusion protein to oil bodies occurred within the first 6 h posttransformation. Oleosin-GFP fusion protein exclusively associated with the endoplasmic reticulum and was trafficked in a Golgi-independent manner at speeds approaching 0.5 microm sec(-1) along highly dynamic endoplasmic reticulum positioned over essentially static polygonal cortical endoplasmic reticulum. Our data indicate that oil body biogenesis can occur outside of the embryo and that oleosin-GFP can be used to monitor early events in oil body biogenesis in real-time.

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Nucleotide sequence of an Arabidopsis thaliana oleosin gene

Cited by 44 publications

References 14 publications

Characterization of a new class of oleosins suggests a male gametophyte specific lipid storage pathway

Characterization of a new class of oleosins suggests a male gametophyte specific lipid storage pathway

Oleosin fusion expression systems for the production of recombinant proteins

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

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