A 10 kD barley basic protein transfers phosphatidylcholine from liposomes to mitochondria

Breu, Volker; Guerbette, F.; Kader, Jean‐Claude; Kannangara, C. Gamini; Svensson, Birte; Wettstein-Knowles, Penny von

doi:10.1007/bf02907587

Cited by 55 publications

(21 citation statements)

References 10 publications

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“…Barley LTP has been demonstrated to transfer phosphatidyl-choline from liposomes to mitochondria in vitro (BREU et al 1989). Three amphiphilic structures in plant LTPs have lengths similar to those of phospholipid acyl chains, and they can form a hydrophobic pocket for the binding of phospholipids, while the hydrophilic surface of the protein renders the protein-lipid complex soluble (MADRID et al 1990;MADRID and VON WETT-STEIN 1991).…”

Section: Discussionmentioning

confidence: 99%

Developmental Patterns of Enzymes and Proteins During Mobilization of Endosperm Stores in Germinating Barley Grains

Jensen

2004

Hereditas

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Mobilization of stored reserves in the endosperm of barley grains involves the interaction of enzymes and other proteins synthesized during grain development and those synthesized during germination. In order to obtain information on this interaction, localization of a-amylase, the bifunctional subtilisinla-amylase inhibitor (BASI), the unspecific lipid transfer protein (LTP), and the antimicrobial proteins chitinase and ribosome inactivating protein (RIP) were determined by immunofluorescence microscopy in the different tissues of resting and germinating grains of the Hordeum uulgare L. genotypes Alexis, Klages, and Steptoe. Targeting of a-amylase from the proximal to the distal part of the endosperm progresses with different rates in the three genotypes. LTP is localized in the endosperms, the aleurone layers and in the embryo of the ungerminated grains. LTP is depleted during the first days of germination but then re-synthesized in the embryo and in the aleurone during the following phases of germination and released to the endosperm independent of cell wall hydrolysis. Chitinase is present in the aleurone layers and, depending on variety, in variable amounts in the endosperm of the mature and the germinating grains. Secretion of chitinase from the aleurone and scutellum is indicated by the increasing amount found in the endosperm during germination. Chitinase accumulates in the distal aleurone layers before a-amylase IS detected and thus must be able to penetrate the intact endosperm 0-glucan walls. BASI and RIP are localized in all parts of the mature grain and at later stages of germination the amount in the scutellum and aleurone layer increases. The analysed enzymes and proteins fulfill different functions during germination and are of importance for the industrial use of the barley crop. The efficient immunohistochemical demonstration of the genotypic bility in these characteristics provides a possibility to identify important breeding targets.

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Section: Discussionmentioning

confidence: 99%

Developmental Patterns of Enzymes and Proteins During Mobilization of Endosperm Stores in Germinating Barley Grains

Jensen

2004

Hereditas

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“…A defense role for these proteins is further supported by evidence of their preferential cell-wall location in epidermal cells throughout the plant and by the increased expression of their genes in response to pathogens [3]. A defense role is not necessarily incompatible with other possible functions, such as lipid exchange between cell organelles in the cytoplasm [4][5][6] or cutin biosynthesis [7,8], and it is becoming increasingly evident that a number of widely divergent LTP subfamilies may coexist in a given plant [2,9], which raises the possibility of a certain degree of functional specialization among these subfamilies. A cytoplasmic role, such as lipid exchange between organelles, would be incompatible with a noncytoplasmic location of the proteins [2,10], so it is of interest to investigate whether LTPs can be also recovered in the soluble fraction.…”

Section: Introduction 2 Materials and Methodsmentioning

confidence: 97%

Purification and antipathogenic activity of lipid transfer proteins (LTPs) from the leaves of Arabidopsis and spinach

Segura¹,

Moreno²,

Garcı́a-Olmedo³

1993

FEBS Letters

125

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Two homogeneous proteins active in vitro against the bacterial pathogen Clavibacter michiganensis subsp. sepedonicus were obtained from a crude cell-wall preparation from the leaves of Columbia wild-type Arabidopsis. The N-terminal amino acid sequences of these proteins allowed their identification as lipid transfer proteins (LTP-al, LTP-a2); the LTPI-al sequence was identical to that deduced from a previously described cDNA (EMBL M80566) and LTP-a2 was quite divergent (44% identical positions). These proteins were not detected in the cytoplasmic fraction by Western-blot analysis. Proteins LTP-sl and LTP-s2 were similarly obtained from spinach leaves; LTP-sl was 91% identical to a previously purified spinach LTP (Swiss Prot PlO976), and LTP-s2 was moderately divergent (71% identical positions). About 113 of the total LTPs were detected in the cytoplasmic fraction from spinach by Western-blot analysis. Concentrations of these proteins causing 50% inhibition (EC-50) were in the 0.1-l yM range for the bacterial pathogens C. michiganensis and Pseudomonas solanacearum and close to 10pM for the fungal pathogen Fusarium solani.

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“…They have also been found in microorganisms and in plants (110). The lipid transfer function of plant LTPs has been reported for spinach leaves (86), maize seedlings (25), barley seeds (15,66), and castor beans (106). They are expressed in the epidermal tissues of a variety of organs including barley aleurone cells (47), leaves and coleoptiles (32), apical meristems (30), and flower buds, but not in roots (83).…”

Section: Movement To the Outer Surfacesmentioning

confidence: 99%

Biochemistry and Molecular Biology of Wax Production in Plants

Post-Beittenmiller

1996

Annu. Rev. Plant. Physiol. Plant. Mol. Biol.

401

273

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The aerial surfaces of plants are covered with a wax layer that is primarily a waterproof barrier but that also provides protection against environmental stresses. The ubiquitous presence of cuticular wax is testimony to its essential function. Genetic and environmental factors influence wax quantity and composition, which suggests that it is an actively regulated process. The basic biochemistry of wax production has been elucidated over the past three decades; however, we still know very little about its regulation. This review presents a discussion along with new perspectives on the regulatory aspects of wax biosynthesis. Among the topics discussed are the partitioning of fatty acid precursors into wax biosynthesis and the elongation of fatty acids with particular emphasis on the nature of the acyl primer, and the role of ATP in fatty acid elongation. The recent cloning of wax biosynthetic genes and the transport of wax to plant surfaces are also discussed. CONTENTS

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A 10 kD barley basic protein transfers phosphatidylcholine from liposomes to mitochondria

Cited by 55 publications

References 10 publications

Developmental Patterns of Enzymes and Proteins During Mobilization of Endosperm Stores in Germinating Barley Grains

Developmental Patterns of Enzymes and Proteins During Mobilization of Endosperm Stores in Germinating Barley Grains

Purification and antipathogenic activity of lipid transfer proteins (LTPs) from the leaves of Arabidopsis and spinach

Biochemistry and Molecular Biology of Wax Production in Plants

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