The amino-acid sequence of the nonspecific lipid transfer protein from germinated castor bean endosperms

Takishima, Kunio; Watanabe, Shinichiro; Yamada, Mitsuhiro; Mamiya, Gunji

doi:10.1016/0167-4838(86)90229-3

Cited by 63 publications

(23 citation statements)

References 22 publications

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“…These results indicate the occurrence of tissue-specific ns-LTPs in castor bean seedlings. The data also provide evidence that the ns-LTP with mol wt 9313 (17), as previously purified from germinated castor bean seeds (22), is mainly located in the cotyledons.…”

Section: Immunoblots Of Ns-ltpssupporting

confidence: 56%

Biosynthesis of Nonspecific Lipid Transfer Proteins in Germinating Castor Bean Seeds

Tsuboi

Watanabe²,

Ozeki³

et al. 1989

Plant Physiol.

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The biosynthesis of nonspecific lipid transfer proteins (nsLTPs) in germinating castor bean (Ricinus communis L.) seeds were investigated. Lipid transfer activities of ns-LTPs in the cotyledons, axis, and endosperm increased with growth after germination. The activity increases were accompanied by increased amounts of ns-LTPs in each tissue, as measured by immunoblot using anti-ns-LTP serum. These results suggest that the ns-LTPs are synthesized de novo in each tissue after germination and not activated from inactive proteins synthesized before germination. Comparison of the immunoblot products in each tissue from 4-day-old seedlings indicate the occurrence of tissuespecific isoforms of ns-LTPs; 9 kilodaltons (major) and 7 kilodaltons (minor) in the cotyledons, and 7 kilodaltons (major) and 9 kilodaltons (minor) in the axis, whereas only the 8-kilodalton ns-LTP is present in the endosperm. In vitro translation from poly(A)+ RNAs from three tissues of castor bean seedlings and the detection of immunoprecipitated products indicate that translatable mRNAs for ns-LTPs exist in the three tissues a day before the synthesis of ns-LTPs; the translation products, which are 3.5 to 4.0 kilodaltons larger than ns-LTPs, were processed to the mature ns-LTPs. The production of mature ns-LTPs from translatable mRNAs without any delay suggests that gene expression of nsLTPs in castor bean seedlings is controlled at a step before the formation of translatable mRNAs.

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Section: Immunoblots Of Ns-ltpssupporting

confidence: 56%

Biosynthesis of Nonspecific Lipid Transfer Proteins in Germinating Castor Bean Seeds

Tsuboi

Watanabe²,

Ozeki³

et al. 1989

Plant Physiol.

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“…Comparison of the EP2 cDNA and amino acid sequences with sequences found in the EMBL DNA sequence and the NBRF and Swiss-Prot protein sequence libraries revealed high sequence homologies with phospholipid transfer proteins from maize (54%; Tchang et al, 1988) and barley (45%; Mundy and Rogers, 1986;Bernhard and Somerville, 1989), respectively. Homology was also found with protein sequences from spinach (49%; Bouillon et al, 1987) and castor bean (Takishima et al, 1986) phospholipid transfer proteins (calculation of percentages based on amino acid sequences as shown in Figure 1D). Due to their aspecific lipid binding properties, these proteins have recently been reclassified as nonspecific lipid transfer proteins (Kader, 1990).…”

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: 90%

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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“…While this study was in progress, the complete structure of a protein, isolated from castor bean seeds, has been elucidated [23]; this protein has a similar property of facilitating a nonspecific transfer of phospholipids [12]. Interestingly the castor bean protein comprises 92 residues, including 8 cysteines; the calculated molecular mass is 9313 Da; in contrast to the spinach protein, 2 phenylalanine residues were found.…”

Section: Discussionmentioning

confidence: 99%

“…This paper reports the complete amino acid sequence of this protein, which is the first phospholipidtransfer protein to be analyzed from a photosynthetic tissue. This structure was compared to that recently obtained with a similar protein purified from castor bean seeds [23]. …”

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confidence: 99%

The primary structure of spinach-leaf phospholipid-transfer protein

et al. 1987

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The complete amino acid sequence phospholipid-transfer protein isolated from spinach leaves has been determined. The primary structure of the spinach protein was elucidated by analyses by HPLC of cyanogen bromide fragments and peptides obtained by tryptic digestions. The single polypeptide chain of the spinach protein consists of 91 amino acid residues. The protein contains six cysteines whereas phenylalanine and glutamine are absent. The present data, which are the first to be obtained with a phospholipid-transfer protein from a photosynthetic tissue, are compared to the amino acid sequences determined with plant and animal proteins involved in the intracellular transport of hydrophobic compounds.Several proteins involved in the intracellular transport or binding of hydrophobic compounds: phospholipids, fatty acids, glycolipids, cholesterol, vitamin A, have been discovered (for reviews, see [l -111. In particular, proteins able to bind or transfer phospholipids, called phospholipid-transfer proteins, have been purified to homogeneity from animals [l -5, 10, 111, higher plants [3,4, 8, 121, yeasts [I31 or bacteria [14]. These proteins have in common the property of facilitating an intermembrane transfer of phospholipids. However, they differ in specificity. Some of these proteins are specific for phosphatidylcholine, like the protein specific to bovine liver [l, 2, 151, or for phosphatidylinositol and phosphatidylcholine, like the bovine brain protein [lo], whereas other proteins are non-specific. Non-specific proteins have been isolated from animal sources (bovine liver [2,4]) or plant tissues (spinach leaf [16], maize seed [17] or castor bean seed [12]); these proteins are for the major part basic (PI around 9 -10). A better knowledge of the structures of these proteins can provide information about their mode of action. The elucidation of the primary structure has only been obtained with two animal phospholipid-transfer proteins: the specific (18, 191 and the non-specific [20, 211 proteins from bovine liver. The recent obtention of high amounts of purified protein from spinach leaf [I61 has allowed a study of its structure; the NH,-terminal end has been determined in previous experiments [22]. This paper reports the complete amino acid sequence of this protein, which is the first phospholipidtransfer protein to be analyzed from a photosynthetic tissue. This structure was compared to that recently obtained with a similar protein purified from castor bean seeds [23]. MATERIALS AND METHODS Purification of phospholipid-transfer proteinPhospholipid transfer protein was isolated from spinach leaves as previously described [16]. The protein was desalted by gel filtration on a column of Sephadex G-25, equilibrated and eluted with 3.5 M acetic acid. Amino acid analysisAmino acid analyses were performed as in [16] on a Technicon TSMl amino acid analyzer. Oxidized protein samples (4 x 1 nmol) were hydrolyzed in 6 M HCl for 24, 48, 72 and 120 h. The values for serine and threonine were determined after 24 h hydrolysis...

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The amino-acid sequence of the nonspecific lipid transfer protein from germinated castor bean endosperms

Cited by 63 publications

References 22 publications

Biosynthesis of Nonspecific Lipid Transfer Proteins in Germinating Castor Bean Seeds

Biosynthesis of Nonspecific Lipid Transfer Proteins in Germinating Castor Bean Seeds

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

The primary structure of spinach-leaf phospholipid-transfer protein

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