Comparison of Lipid Binding and Transfer Properties of Two Lipid Transfer Proteins from Plants

Guerbette, F.; Grosbois, Michèle; Jolliot-Croquin, Alain; Kader, Jean‐Claude; Zachowski, Alain

doi:10.1021/bi990952l

Cited by 44 publications

(35 citation statements)

References 47 publications

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“…To isolate wheat (Triticum aestivum) LTP, we used a conventional procedure (Guerbette et al, 1999) but avoided the generally used reversephase chromatography, because this method involves hydrophobic solvents that may occupy the hydrophobic cavity of LTP. In short, the procedure was as follows.…”

Section: Wheat Ltp Purificationmentioning

confidence: 99%

Lipid Transfer Proteins Enhance Cell Wall Extension in Tobacco

et al. 2005

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Plant cells are enclosed by a rigid cell wall that counteracts the internal osmotic pressure of the vacuole and limits the rate and direction of cell enlargement. When developmental or physiological cues induce cell extension, plant cells increase wall plasticity by a process called loosening. It was demonstrated previously that a class of proteins known as expansins are mediators of wall loosening. Here, we report a type of cell wall-loosening protein that does not share any homology with expansins but is a member of the lipid transfer proteins (LTPs). LTPs are known to bind a large range of lipid molecules to their hydrophobic cavity, and we show here that this cavity is essential for the cell wall-loosening activity of LTP. Furthermore, we show that LTP-enhanced wall extension can be described by a logarithmic time function. We hypothesize that LTP associates with hydrophobic wall compounds, causing nonhydrolytic disruption of the cell wall and subsequently facilitating wall extension.

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Section: Wheat Ltp Purificationmentioning

confidence: 99%

Lipid Transfer Proteins Enhance Cell Wall Extension in Tobacco

et al. 2005

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“…It is also clear that the lipidbinding properties differ significantly between LTPs from various sources. For instance, it was recently shown that wheat LTP had lower transfer activity and lower kinetics for fatty acid binding in comparison with a maize LTP (Guerbette et al 1999). These differences in lipid binding were attributed to structural differences in the binding cavities of the proteins.…”

Section: Introductionmentioning

confidence: 99%

Characterization of germination-specific lipid transfer proteins from Euphorbia lagascae

Edqvist

Farbos

2002

Planta

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The endosperm of Euphorbia lagascae Spreng. seeds contains high levels of the epoxidated fatty acid vernolic acid ( cis-12-epoxyoctadeca-cis-9-enoic acid). To obtain transgenic oilcrops producing high levels of vernolic acid, better knowledge of its endogenous metabolism is needed. In this paper we study the gene activities involved in the mobilization and oxidation of vernolic acid during germination. A cDNA library was constructed from mRNA isolated from germinating E. lagascae seeds. Over 300 cDNA clones were partially characterized by DNA sequencing. Of the sequenced cDNAs, 18% encoded proteins with a putative function related to the metabolism of lipids or fatty acids. Among these cDNAs were genes coding for lipase, thiolase, acyl-CoA reductase and epoxide hydrolase. Of the sequenced clones, 4.5% encoded lipid-transfer proteins (LTPs), indicating the high abundance of such proteins during germination. We isolated the full-length sequences of the E. lagascae cDNAs encoding the LTPs ElLTP1 and ElLTP2. These proteins share only 38% identity, but both show high similarity to LTPs from other plant species. Both sequences contain eight cysteine residues, which are conserved in most plant LTPs. Expression analysis revealed that both genes were specifically expressed during germination.

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“…21 Investigations from non-plant sources suggest that phospholipid transfer from the ER to other intracellular membranes are mediated by cytosolic lipid transfer proteins and currently little is known of such proteins operating in plants. 20,[22][23][24] Since ACBP6 can bind PC in vitro, we propose that ACBP6 is a possible candidate in the cytosolic binding and trafficking of PC in plant cells. The in vivo lipid-transfer activity of ACBP6 and its significance in PC-trafficking in planta await further investigations using in vivo and in vitro experiments.…”

Section: Discussionmentioning

confidence: 98%