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. 1991 Sep;3(9):907–921. doi: 10.1105/tpc.3.9.907

Cell-specific expression of the carrot EP2 lipid transfer protein gene.

P Sterk 1, H Booij 1, G A Schellekens 1, A Van Kammen 1, S C De Vries 1
PMCID: PMC160059  PMID: 1822991

Abstract

A cDNA corresponding to a 10-kD protein, designated extracellular protein 2 (EP2), that is secreted by embryogenic cell cultures of carrot was obtained by expression screening. The derived protein sequence and antisera against heterologous plant lipid transfer proteins identified the EP2 protein as a lipid transfer protein. Protein gel blot analysis showed that the EP2 protein is present in cell walls and conditioned medium of cell cultures. RNA gel blot analysis revealed that the EP2 gene is expressed in embryogenic cell cultures, the shoot apex of seedlings, developing flowers, and maturing seeds. In situ hybridization showed expression of the EP2 gene in protoderm cells of somatic and zygotic embryos and transient expression in epidermis cells of leaf primordia and all flower organs. In the shoot apical meristem, expression is found in the tunica and lateral zone. In maturing seeds, the EP2 gene is expressed in the outer epidermis of the integument, the seed coat, and the pericarp epidermis, as well as transiently in between both mericarps. Based on the extracellular location of the EP2 protein and the expression pattern of the encoding gene, we propose a role for plant lipid transfer proteins in the transport of cutin monomers through the extracellular matrix to sites of cutin synthesis.

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Selected References

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  1. Arondel V., Kader J. C. Lipid transfer in plants. Experientia. 1990 Jun 15;46(6):579–585. doi: 10.1007/BF01939696. [DOI] [PubMed] [Google Scholar]
  2. Bernhard W. R., Somerville C. R. Coidentity of putative amylase inhibitors from barley and finger millet with phospholipid transfer proteins inferred from amino acid sequence homology. Arch Biochem Biophys. 1989 Mar;269(2):695–697. doi: 10.1016/0003-9861(89)90154-9. [DOI] [PubMed] [Google Scholar]
  3. Bernhard W. R., Thoma S., Botella J., Somerville C. R. Isolation of a cDNA Clone for Spinach Lipid Transfer Protein and Evidence that the Protein Is Synthesized by the Secretory Pathway. Plant Physiol. 1991 Jan;95(1):164–170. doi: 10.1104/pp.95.1.164. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Borkird C., Choi J. H., Jin Z. H., Franz G., Hatzopoulos P., Chorneau R., Bonas U., Pelegri F., Sung Z. R. Developmental regulation of embryonic genes in plants. Proc Natl Acad Sci U S A. 1988 Sep;85(17):6399–6403. doi: 10.1073/pnas.85.17.6399. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bouillon P., Drischel C., Vergnolle C., Duranton H., Kader J. C. The primary structure of spinach-leaf phospholipid-transfer protein. Eur J Biochem. 1987 Jul 15;166(2):387–391. doi: 10.1111/j.1432-1033.1987.tb13527.x. [DOI] [PubMed] [Google Scholar]
  6. Choi J. H., Liu L. S., Borkird C., Sung Z. R. Cloning of genes developmentally regulated during plant embryogenesis. Proc Natl Acad Sci U S A. 1987 Apr;84(7):1906–1910. doi: 10.1073/pnas.84.7.1906. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Dure L., 3rd, Greenway S. C., Galau G. A. Developmental biochemistry of cottonseed embryogenesis and germination: changing messenger ribonucleic acid populations as shown by in vitro and in vivo protein synthesis. Biochemistry. 1981 Jul 7;20(14):4162–4168. doi: 10.1021/bi00517a033. [DOI] [PubMed] [Google Scholar]
  8. Kader J. C., Julienne M., Vergnolle C. Purification and characterization of a spinach-leaf protein capable of transferring phospholipids from liposomes to mitochondria or chloroplasts. Eur J Biochem. 1984 Mar 1;139(2):411–416. doi: 10.1111/j.1432-1033.1984.tb08020.x. [DOI] [PubMed] [Google Scholar]
  9. Lo Schiavo F., Giuliano G., de Vries S. C., Genga A., Bollini R., Pitto L., Cozzani F., Nuti-Ronchi V., Terzi M. A carrot cell variant temperature sensitive for somatic embryogenesis reveals a defect in the glycosylation of extracellular proteins. Mol Gen Genet. 1990 Sep;223(3):385–393. doi: 10.1007/BF00264444. [DOI] [PubMed] [Google Scholar]
  10. Perez-Grau L., Goldberg R. B. Soybean Seed Protein Genes Are Regulated Spatially during Embryogenesis. Plant Cell. 1989 Nov;1(11):1095–1109. doi: 10.1105/tpc.1.11.1095. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Somerharju P. J., van Paridon P. A., Wirtz K. W. Application of fluorescent phospholipid analogues to studies on phospholipid transfer proteins. Subcell Biochem. 1990;16:21–43. doi: 10.1007/978-1-4899-1621-1_2. [DOI] [PubMed] [Google Scholar]
  12. Tchang F., This P., Stiefel V., Arondel V., Morch M. D., Pages M., Puigdomenech P., Grellet F., Delseny M., Bouillon P. Phospholipid transfer protein: full-length cDNA and amino acid sequence in maize. Amino acid sequence homologies between plant phospholipid transfer proteins. J Biol Chem. 1988 Nov 15;263(32):16849–16855. [PubMed] [Google Scholar]
  13. von Heijne G. Patterns of amino acids near signal-sequence cleavage sites. Eur J Biochem. 1983 Jun 1;133(1):17–21. doi: 10.1111/j.1432-1033.1983.tb07424.x. [DOI] [PubMed] [Google Scholar]

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