Characterization of germination-specific lipid transfer proteins from Euphorbia lagascae

Edqvist, Johan; Farbos, Isabelle

doi:10.1007/s00425-001-0717-x

Cited by 33 publications

(32 citation statements)

References 32 publications

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“…The expression pattern of AtSCP-2 is, thus, not suggestive of that the main role of the protein is in the peroxisomes during seed germination. Although, support for a role of plant SCP-2 during germination comes from the original identification of E. lagascae SCP-2 protein and mRNA in the endosperm of germinating seeds (34,48).…”

Section: Table I Scp-2 In Vitro Normalized Lipid Transfer Activitymentioning

confidence: 99%

Plants Express a Lipid Transfer Protein with High Similarity to Mammalian Sterol Carrier Protein-2

Edqvist

Rönnberg

Rosenquist

et al. 2004

Journal of Biological Chemistry

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This is the first report describing the cloning and characterization of sterol carrier protein-2 (SCP-2) from plants. Arabidopsis thaliana SCP-2 (AtSCP-2) consists of 123 amino acids with a molecular mass of 13.6 kDa. AtSCP-2 shows 35% identity and 56% similarity to the human SCP-2-like domain present in the human D-bifunctional protein (DBP) and 30% identity and 54% similarity to the human SCP-2 encoded by SCP-X. The presented structural models of apo-AtSCP-2 and the ligandbound conformation of AtSCP-2 reveal remarkable similarity with two of the structurally known SCP-2s, the SCP-2-like domain of human DBP and the rabbit SCP-2, correspondingly. The AtSCP-2 models in both forms have a similar hydrophobic ligand-binding tunnel, which is extremely suitable for lipid binding. AtSCP-2 showed in vitro transfer activity of BODIPYphosphatidylcholine (BODIPY-PC) from donor membranes to acceptor membranes. The transfer of BODIPY-PC was almost completely inhibited after addition of 1-palmitoyl 2-oleoyl phosphatidylcholine or ergosterol. Dimyristoyl phosphatidic acid, stigmasterol, steryl glucoside, and cholesterol showed a moderate to marginal ability to lower the BODIPY-PC transfer rate, and the single chain palmitic acid and stearoyl-coenzyme A did not affect transfer at all. Expression analysis showed that AtSCP-2 mRNA is accumulating in most plant tissues. Plasmids carrying fusion genes between green fluorescent protein and AtSCP-2 were transformed with particle bombardment to onion epidermal cells. The results from analyzing the transformants indicate that AtSCP-2 is localized to peroxisomes.

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Section: Table I Scp-2 In Vitro Normalized Lipid Transfer Activitymentioning

confidence: 99%

Plants Express a Lipid Transfer Protein with High Similarity to Mammalian Sterol Carrier Protein-2

Edqvist

Rönnberg

Rosenquist

et al. 2004

Journal of Biological Chemistry

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“…Concerning plant development, it has been suggested that LTPs are involved in the mobilization of seed storage lipids (3), in the formation of cuticles (4,5), in pollen tube adhesion (6,7), in endosperm programmed cell death (8), and in cell wall loosening (9). Concerning plant defense against biotic and abiotic stress, it has been shown that LTPs are associated with cold and wounding stress (10,11), are induced by microbial pathogens (12), and can inhibit fungal growth in vitro (13,14).…”

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confidence: 99%

Specific Adduction of Plant Lipid Transfer Protein by an Allene Oxide Generated by 9-Lipoxygenase and Allene Oxide Synthase

Bakan

Hámberg

Perrocheau

et al. 2006

Journal of Biological Chemistry

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Lipid transfer proteins (LTPs) are ubiquitous plant lipidbinding proteins that have been associated with multiple developmental and stress responses. Although LTPs typically bind fatty acids and fatty acid derivatives in a non-covalent way, studies on the LTPs of barley seeds have identified an abundantly occurring covalently modified form, LTP1b, the lipid ligand of which has resisted clarification. In the present study, this adduct was identified as the ␣-ketol 9-hydroxy-10-oxo-12(Z)-octadecenoic acid. Further studies on the formation of LTP1b demonstrated that the ligand was introduced by nucleophilic attack of the free carboxylate group of the Asp-7 residue of the protein at carbon-9 of the allene oxide fatty acid 9(S),10-epoxy-10,12(Z)-octadecadienoic acid. This reactive oxylipin was produced in barley seeds by oxygenation of linoleic acid by 9-lipoxygenase followed by dehydration of the resulting hydroperoxide by allene oxide synthase. The generation of protein-oxylipin adducts represents a new function for plant allene oxide synthases, enzymes that have earlier been implicated mainly in the biosynthesis of the jasmonate family of plant hormones. Additionally, the LTP-allene oxide synthase interaction opens new perspectives regarding the roles of LTPs in the signaling of plant defense and development.

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“…Non-specific LTPs (nsLTP) may have a range of biological functions including antimicrobial role in plant defence, systemic acquired resistance pathway, seed germination, anther development etc. (Buhot et al 2001;Maldonado et al 2002;Edqvist and Farbos 2002). Several LTP proteins were shown to be upregulated during late petal formation in the flowers of Gerbera (Laitinen et al 2005).…”

Section: Discussionmentioning

confidence: 98%

Os11Gsk gene from a wild rice, Oryza rufipogon improves yield in rice

Thalapati

Batchu

Neelamraju

et al. 2012

Funct Integr Genomics

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Chromosomal segments from wild rice species Oryza rufipogon, introgressed into an elite indica rice restorer line (KMR3) using molecular markers, resulted in significant increase in yield. Here we report the transcriptome analysis of flag leaves and fully emerged young panicles of one of the high yielding introgression lines IL50-7 in comparison to KMR3. A 66-fold upregulated gene Os11Gsk, which showed no transcript in KMR3 was highly expressed in O. rufipogon and IL50-7. A 5-kb genomic region including Os11Gsk and its flanking regions could be PCR amplified only from IL50-7, O. rufipogon, japonica varieties of rice-Nipponbare and Kitaake but not from the indica varieties, KMR3 and Taichung Native-1. Three sister lines of IL50-7 yielding higher than KMR3 showed presence of Os11Gsk, whereas the gene was absent in three other ILs from the same cross having lower yield than KMR3, indicating an association of the presence of Os11Gsk with high yield. Southern analysis showed additional bands in the genomic DNA of O. rufipogon and IL50-7 with Os11Gsk probe. Genomic sequence analysis of ten highly co-expressed differentially regulated genes revealed that two upregulated genes in IL50-7 were derived from O. rufipogon and most of the downregulated genes were either from KMR3 or common to KMR3, IL50-7, and O. rufipogon. Thus, we show that Os11Gsk is a wild rice-derived gene introduced in KMR3 background and increases yield either by regulating expression of functional genes sharing homology with it or by causing epigenetic modifications in the introgression line.

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Characterization of germination-specific lipid transfer proteins from Euphorbia lagascae

Cited by 33 publications

References 32 publications

Plants Express a Lipid Transfer Protein with High Similarity to Mammalian Sterol Carrier Protein-2

Plants Express a Lipid Transfer Protein with High Similarity to Mammalian Sterol Carrier Protein-2

Specific Adduction of Plant Lipid Transfer Protein by an Allene Oxide Generated by 9-Lipoxygenase and Allene Oxide Synthase

Os11Gsk gene from a wild rice, Oryza rufipogon improves yield in rice

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