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

Bernhard, Werner; Thoma, Sharon; Botella, José Ramón; Somerville, Chris

doi:10.1104/pp.95.1.164

Cited by 121 publications

(61 citation statements)

References 29 publications

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“…The gene consists of two exons coding for 11 2 and two amino acids separated by a 980 bp intron. The first 23 amino acids have the properties of a signal sequence, as is the case for other LTP genes (Bernhard and Somerville, 1989;Bernhard et a/., 1991;Sterk et al, 1991 ;Tchang et a/., 1988). The predicted mature protein has a molecular mass of 91 54 and a pl of 11.3.…”

Section: /Solation Of Tobacco Ltp Genesmentioning

confidence: 99%

Expression pattern of a tobacco lipid transfer protein gene within the shoot apex

et al. 1992

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SummaryA genomic clone coding for a putative lipid transfer protein was isolated from Nicotiana tabacurn. The gene is expressed in all aerial organs of the tobacco plant, with expression being highest in the upper part of the plant and declining towards the base (i.e. with increasing age). In the shoot apex transcript levels are highest in the LI layer, lower in the underlying cell layers, and are again higher in the submeristem region. This pattern is markedly different from those previously described for genes expressed within the shoot apex.

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Section: /Solation Of Tobacco Ltp Genesmentioning

confidence: 99%

Expression pattern of a tobacco lipid transfer protein gene within the shoot apex

et al. 1992

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“…Amino acid sequence alignment between mature Ace-AMP1 and nsLTPs or nsLTP-like proteins. The following sequences of nsLTPs or nsLTP-like proteins are included in the comparison: Rs-nsLTP from Raphanus sativus seeds (Terras et al, 1992a); So-nsLTP from Spinacia oleracea leaves (Bernhard et al, 1991); EP2 from Daucus carota zygotic embryos (Sterk et al, 1991); TobLTP from Nicotiana tabacum flowers (Masuta et al, 1992); Le-nsLTP from Lycopersicon esculentum (Torres-Schumann et al, 1992); CB-A, CB-B, and CB-C from Ricinus communis seedlings (Takishima et al, 1988); PAPI from Hordeum vulgare seeds (Mundy and Rogers, 1986); CW18 and CW21 from Hordeum vulgare leaves (Molina et ai., 1993); Ta-nsLTP from Triticum aestivum seeds (Simorre et al, 1991); and Zm-nsLTP from Zea mays seedlings (Tchang et al, 1988). Gaps introduced for optimal alignment are indicated by dashes and question marks represent unknown residues.…”

Section: Aitcgqvssalgpcaayakgsstspsa-gccsgvkrlaglarstadkqatcclksvagaymentioning

confidence: 99%

A Potent Antimicrobial Protein from Onion Seeds Showing Sequence Homology to Plant Lipid Transfer Proteins

et al. 1995

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An antimicrobial protein of about 1 O kD, called AceAMPl, was isolated from onion (Allium cepa L.) seeds. Based on the nearcomplete amino acid sequence of this protein, oligonucleotides were designed for polymerase chain reaction-based cloning of the corresponding cDNA. l h e mature protein is homologous t o plant nonspecific lipid transfer proteins (nsLTPs), but it shares only 76% of the residues that are conserved among all known plant nsLTPs and is unusually rich in arginine. AceAMP1 inhibits all 12 tested plant pathogenic fungi at concentrations below 10 pg mL-'. Its antifungal activity is either not at all or is weakly affected by the presence of different cations at concentrations approximating physiological ionic strength conditions. AceAMP1 is also active on two Cram-positive bacteria but is apparently not toxic for Cram-negative bacteria and cultured human cells. In contrast t o nsLTPs such as those isolated from radish or maize seeds, AceAMPI was unable t o transfer phospholipids from liposomes to mitochondria. On the other hand, lipid transfer proteins from wheat and maize seeds showed little or no antimicrobial activity, whereas the radish lipid transfer protein displayed antifungal activity only in media with low cation concentrations. l h e relevance of these findings with regard to the function of nsLTPs is discussed.Although plant seeds are usually sown on a substrate that is extremely rich in microorganisms, infection of seeds or seedling tissues normally occurs at relatively low frequency. It is believed that seed proteins that exhibit antimicrobial activity may participate in the protection of seeds against potential microbial invaders. Different types of antimicrobial proteins have been purified from plant seeds '

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“…The predicted existence of a signal peptide was supported by the fact that all homologous N-terminal protein sequences of the mature protein commenced at the predicted cleavage site of the EP2 protein. In addition, the homologous cDNAs from maize (Tchang et al, 1988) and spinach (Bernhard et al, 1991) have a 27 amino acid signal peptide ending precisely at the equivalent position of the predicted EP2 cleavage site. All protein sequences show conservation of six to eight cysteines as well as two or three charged amino acids present at positions 45 to 47, as counted from the presumed signal sequence cleavage site.…”

Section: T G C T G G C C T C C C T G C T a G A T G T G G T G T C~c~t mentioning

confidence: 99%

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

et al. 1991

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

Cited by 121 publications

References 29 publications

Expression pattern of a tobacco lipid transfer protein gene within the shoot apex

Expression pattern of a tobacco lipid transfer protein gene within the shoot apex

A Potent Antimicrobial Protein from Onion Seeds Showing Sequence Homology to Plant Lipid Transfer Proteins

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

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