Synthesis of phospholipid transfer proteins from maize seedlings

Vergnolle, Chantal; Arondel, Vincent; Tchang, Françoise; Grosbois, Michèle; Guerbette, F.; Jolliot, Alain; Kader, Jean‐Claude

doi:10.1016/s0006-291x(88)80007-x

Cited by 21 publications

(16 citation statements)

References 14 publications

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“…Thus, the evidence indicates that the mature lipid transfer protein is sequestered in the endoplasmic reticulum. This result is consistent with the results of recent experiments indicating that maize lipid transfer protein is synthesized on membranebound polysomes (24).…”

Section: In Vitro Translation and Processingsupporting

confidence: 93%

Isolation of a cDNA Clone for Spinach Lipid Transfer Protein and Evidence that the Protein Is Synthesized by the Secretory Pathway

Bernhard¹,

Thoma²,

Botella³

et al. 1991

Plant Physiol.

121

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(10,12,29). Under conditions in which the donor membrane is actively engaged in lipid synthesis, plant lipid transfer proteins have also been shown to catalyze net transfer from the donor to acceptor membrane ( 17). On this basis, it has been proposed that they participate in the transfer of lipids between membranes in intact cells (17). However, this family of proteins is relatively poorly characterized in several respects, and a role in intracellular lipid transport is not established (2).

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Section: In Vitro Translation and Processingsupporting

confidence: 93%

Isolation of a cDNA Clone for Spinach Lipid Transfer Protein and Evidence that the Protein Is Synthesized by the Secretory Pathway

Bernhard¹,

Thoma²,

Botella³

et al. 1991

Plant Physiol.

121

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“…Equal amounts of total RNAs from the following two samples were analyzed: (1) isolated embryos (scutellum and embryonic axis), and (2) endosperms (with aleurone tissues, without periderm). Blots were hybridized with the 9C2 cDNA probe, which corresponds to the maize LTP gene (Tchang et al, 1988). As shown in Figure 1 A, for each developmental stage and each tissue, the probe hybridized with an abundant 0.9-kb mRNA.…”

Section: Ltp Mrnas Accumulate During Seed Maturationmentioning

confidence: 99%

“…The sequence of a fulllength cDNA encoding maize LTP indicates the presence of a leader peptide of 27 residues (Tchang et al, 1988). This peptide has characteristics of signal peptides and may allow membrane transit.…”

Section: Ltp 1s Heterogeneously Distributed Within Organsmentioning

confidence: 99%

“…They exhibit similar properties: (1) a high pl (9 to 1 O), (2) a molecular mass of approximately 9 kD (90 to 93 amino acids), (3) high sequence homologies including the presente of 8 cysteine residues at conserved locations, and (4) a broad specificity for lipids (Kader et al, 1984;Watanabe and Yamada, 1986;Kader, 1990). cDNAs encoding LTPs have been isolated and characterized from maize seedlings (Tchang et al, 1988), spinach leaves (Bernhard et al, 1991), and barley (Mundy and Rogers, 1986;Breu et al, 1989). Because of their ability to transfer lipids in vitro, LTPs are assumed to play a role in membrane ' To whom correspondence should be addressed.…”

Section: Introductionmentioning

confidence: 99%

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Spatial and Temporal Expression of a Maize Lipid Transfer Protein Gene

Sossountzov¹,

Ruiz-Avila²,

Vignols³

et al. 1991

The Plant Cell

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We studied the temporal and spatial pattern of lipid transfer protein (LTP) gene expression, as well as the localization of this protein, in maize. Using an LTP gene, we observed an accumulation of LTP mRNA in embryos and endosperms during seed maturation. LTP gene expression was also investigated in young seedlings. After germination, the leve1 of LTP mRNA in the coleoptile increased, with a maximum at 7 days, whereas LTP mRNA levels were low in the scutellum and negligible in roots. The high levels of LTP mRNA found in coleoptiles and embryos were confirmed by in situ hybridization. Moreover, LTP gene expression appeared to be localized in the externa1 cellular layers and around the leaf veins. Using immunogold methods, we also observed that LTP was distributed heterogeneously in the different cells of coleoptiles and leaves. The highest concentrations of LTP were found in the outer epidermis of the coleoptiles as well as in the leaf veins. Together, our observations indicate that LTP gene expression is not only organ specific and time specific but also cell specific.

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“…tion, there is evidence for nsLTP having an amino-terminal extension and being synthesized on membrane-bound polysomes Vergnolle et al, 1988). Also, spinach nsLTP contains a signal peptide and is cotranslationally inserted into microsomal membranes (Bernhard & Sommerville, 1989).…”

mentioning

confidence: 99%

Structure in solution of a four‐helix lipid binding protein

et al. 1996

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Because of the low solubility of lipids in water, intercellular and intracellular pathways of lipid transfer are necessary, e.g., for membrane formation. The mechanism by which lipids in vivo are transported from their site of biogenesis (endoplasmatic reticulum and the chloroplasts) to their place of action is unknown. Several small plant proteins with the ability to mediate transfer of radiolabeled phospholipids in vitro from liposomal donor membranes to mitochondrial and chloroplast acceptor membranes have been isolated, and a protein with this ability, the nonspecific lipid transfer protein (nsLTP) isolated from barley seeds (bLTP), has been studied here. The structure and the protein lipid interactions of lipid transfer proteins are relevant for the understanding of their function, and here we present the three-dimensional structure in solution of bLTP as determined by NMR spectroscopy. The ' H NMR spectrum of the 91-residue protein was assigned for more than 97% of the protein ' H atoms, and the structure was calculated on the basis of 813 distance restraints from 'H-'H nuclear Overhauser effects, four disulfide bond restraints, from dihedral angle restraints for 66 @-angles, 61 x' angles, and 2 x ' angles, and from 31 sets of hydrogen bond restraints. The solution structure of bLTP consists of four well-defined a-helices A-D (A, Cys 3-Gly 19; B, Gly 25-Ala 38; C, Arg 44-Gly 57; D, Leu 63-Cys 73), separated by three short loops that are less well defined and concluded by a well defined C-terminal peptide segment with no observable regular secondary structure. For the 17 structures that are used to represent the solution structure of bLTP, the RMS deviation to an average structure is 0.63 A f 0.04 A for backbone atoms and 0.93 A k 0.06 A for all heavy atoms. The secondary structure elements and their locations in the sequence resemble those of nsLTP from two other plant species, wheat and maize, whose structures were previously determined (Gincel E et al, 1995, Eur JBiochern 226:413-422; Shin DH et al, 1995, Structure3: 189-199). In bLTP, the residues analogous to those in maize nsLTP that constitute the palmitate binding site are forming a similar hydrophobic cavity and a potential acyl group binding site. Analysis of the solution structure of bLTP and bLTP in complex with a ligand might provide information on the conformational changes in the protein upon ligand binding and subsequently provide information on the mode of ligand uptake and release. In this work, we hope to establish a foundation for further work of determining the solution structure of bLTP in complex with palmitoyl coenzyme A, which is a suitable ligand, and subsequently to outline the mode of ligand binding.

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Synthesis of phospholipid transfer proteins from maize seedlings

Cited by 21 publications

References 14 publications

Isolation of a cDNA Clone for Spinach Lipid Transfer Protein and Evidence that the Protein Is Synthesized by the Secretory Pathway

Isolation of a cDNA Clone for Spinach Lipid Transfer Protein and Evidence that the Protein Is Synthesized by the Secretory Pathway

Spatial and Temporal Expression of a Maize Lipid Transfer Protein Gene

Structure in solution of a four‐helix lipid binding protein

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