Acid Phosphatase-1 from Nematode Resistant Tomato

Williamson, Valerie M.; Colwell, Greggory W.

doi:10.1104/pp.97.1.139

Cited by 46 publications

(21 citation statements)

References 13 publications

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“…The apparent low abundance suggests that they may not play an important storage role in Arabidopsis as they do in soybean. Recently, it was reported that tomato contains low amounts of an acid phosphatase that has about 45% sequence identity with soybean VSP (20). The function of the Arabidopsis polypeptides that react with the VSP antiserum remains to be determined.…”

Section: Discussionmentioning

confidence: 99%

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Methyl jasmonate inhibition of root growth and induction of a leaf protein are decreased in an Arabidopsis thaliana mutant.

Staswick

Howell

1992

Proc. Natl. Acad. Sci. U.S.A.

761

625

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Jasmonic acid and its methyl ester, methyl jasmonate (MeJA), are plant signaling molecules that affect plant growth and gene expression. Primary root growth of wild-type Arabidopsis thaliana seedlings was inhibited 50% when seedlings were grown on agar medium containing 0.1 IAMMeJA. An ethyl methanesulfonate mutant (jarn) with decreased sensitivity to MeJA inhibition of root elongation was isolated and characterized. Genetic data indicated the trait was recessive and controlled by a single Mendelian factor. MeJAinduced polypeptides were detected in Arabidopsis leaves by antiserum to a MeJA-inducible vegetative storage protein from soybean. The induction of these proteins by MeJA in the mutant was at least 4-fold less in jar] compared to wild type. In contrast, seeds ofjarl plants were more sensitive than wild type to inhibition of germination by abscisic acid. These results suggest that the defect in jar) affects a general jasmonate response pathway, which may regulate multiple genes in different plant organs.Jasmonate is an endogenous plant compound that affects growth and was recently recognized for its ability to induce the expression of specific plant genes. Methyl jasmonate (MeJA), the methyl ester ofjasmonic acid (JA), is one of the few plant compounds that is effective as a vapor at low concentrations, inducing tomato leaf proteinase inhibitors (1) and soybean leaf vegetative storage proteins (VSPs) (2). These two protein classes are also wound-inducible and recent results indicate that MeJA induces the phytoalexin plant defense pathway in several species (3). This evidence suggests that jasmonate may be an important stress-signaling molecule in plants.Jasmonate is derived from the lipoxygenase-dependent oxidation of linolenic acid (4). By analogy with the production of various eicosanoids involved in animal stress signaling (e.g., prostaglandins), it has been suggested that JA arises from the release of cell membrane fatty acids through the action of lipase in response to wounding or autolytic events (5, 6). MeJA also has pheromone activity in at least one insect (7) and is found in certain fungi. Thus, jasmonate is of general biological interest.Evidence that de novo synthesis ofjasmonate plays a role in regulating soybean VSP genes in response to wounding was recently reported (8). However, little is known about the signal-transduction mechanism for jasmonate action in plants. Mutants in phytohormone synthesis and response have received increased attention in recent years. Such mutants not only provide a better understanding of plant growth regulator function but, with emerging technology, may provide a strategy for the isolation of genes involved in plant hormone signaling pathways (9, 10). The purpose of this study was to find and characterize Arabidopsis mutants with an altered response to MeJA. METHODS 6837The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely...

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Section: Discussionmentioning

confidence: 99%

“…We also examined root growth in these mutants in the presence of 20 AM MeJA. Roots of the ABA-insensitive mutants were inhibited to about the same extent as wild type, whereas jarl roots were twice as long after growth on MeJA.…”

Section: Discussionmentioning

confidence: 99%

Methyl jasmonate inhibition of root growth and induction of a leaf protein are decreased in an Arabidopsis thaliana mutant.

Staswick

Howell

1992

Proc. Natl. Acad. Sci. U.S.A.

761

625

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“…These contrasting expression patterns can be interpreted by the assumption that Arabidopsis VSPs may have other functions beyond a temporary protein reserve. A number of plant acid phosphatases have been implicated in resistance to pathogens and nematodes (Williamson and Colwell, 1991;Beßer et al, 2000;Jakobek and Lindgren, 2002;Petters et al, 2002;Stenzel et al, 2003). They appear to be induced by different regulatory pathways; barley acid phosphatase was induced by the salicylic acid mimic 2,6-dichloroisonicotinic acid and JA, while potato acid phosphatase responded only to intact bacterial organisms.…”

Section: Defense: One Possible Biological Function In Planta For Atvspmentioning

confidence: 99%

Arabidopsis Vegetative Storage Protein Is an Anti-Insect Acid Phosphatase

Liu

Ahn²,

Datta³

et al. 2005

Plant Physiology

152

116

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Indirect evidence previously suggested that Arabidopsis (Arabidopsis thaliana) vegetative storage protein (VSP) could play a role in defense against herbivorous insects. To test this hypothesis, other AtVSP-like sequences in Arabidopsis were identified through a Basic Local Alignment Search Tool search, and their transcriptional profiles were investigated. In response to methyl jasmonate application or phosphate starvation, AtVSP and AtVSP-like genes exhibited differential expression patterns, suggesting distinct roles played by each member. Arabidopsis VSP2 (AtVSP2), a gene induced by wounding, methyl jasmonate, insect feeding, and phosphate deprivation, was selected for bacterial expression and functional characterization. The recombinant protein exhibited a divalent cation-dependent phosphatase activity in the acid pH range. When incorporated into the diets of three coleopteran and dipteran insects that have acidic gut lumen, recombinant AtVSP2 significantly delayed development of the insects and increased their mortality. To further determine the biochemical basis of the anti-insect activity of the protein, the nucleophilic aspartic acid-119 residue at the conserved DXDXT signature motif was substituted by glutamic acid via site-directed mutagenesis. This single-amino acid alteration did not compromise the protein's secondary or tertiary structure, but resulted in complete loss of its acid phosphatase activity as well as its anti-insect activity. Collectively, we conclude that AtVSP2 is an anti-insect protein and that its defense function is correlated with its acid phosphatase activity.

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“…pH 3.5-4. The cloned gene for the tomato APase isozyme exhibited homology to vegetative storage proteins (VSPs; Williamson and Colwell 1991). A soybean root nodule APase also shared homology to VSPs (Penheiter et al 1997).…”

Section: Discussionmentioning

confidence: 99%

Isolation and partial characterisation of acid phosphatase isozymes from dormant oilseed of Corylus avellana L.

Andriotis

Ross

2004

Planta

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The acid phosphatase (orthophosphoric-monoester phosphohydrolase, EC 3.1.3.2) complement from dormant hazel (Corylus avellana L.) seeds was found to exhibit significant electrophoretic heterogeneity partially attributable to the presence of distinct molecular forms. In axiferous tissue, total acid phosphatase activity increased in a biphasic fashion during chilling, a treatment necessary to alleviate seed dormancy. Three acid phosphatase isozymes were isolated from cotyledons of dormant hazel seeds by successive ammonium sulphate precipitation, size-exclusion, Concanavalin A affinity, cation- and anion-exchange chromatographies resulting in 75-, 389- and 191-fold purification (APase1, APase2, APase3, respectively). The three glycosylated isoforms were isolated to catalytic homogeneity as determined by electrophoretic, kinetic and heat-inactivation studies. The native acid phosphatase complement of hazel seeds had an apparent Mr of 81.5 +/- 3.5 kDa as estimated by size-exclusion chromatography, while the determined pI values were 5.1 (APase1), 6.9 (APase2) and 7.3 (APase3). The optimum pH for p-nitrophenyl phosphate hydrolysis was pH 3 (APase1), pH 5.6 (APase2) and pH 6 (APase3). The hazel isozymes hydrolysed a variety of phosphorylated substrates in a non-specific manner, exhibiting low Km and the highest specificity constant (Vmax/ Km) for pyrophosphate. They were not primary phytases since they could not initiate phytic acid hydrolysis, while APase2 and APase3 had significant phospho-tyrosine phosphatase activity. Inorganic phosphate was a competitive inhibitor, while activity was significantly impaired in the presence of vanadate and fluoride.

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Acid Phosphatase-1 from Nematode Resistant Tomato

Abstract: Aps-1 encodes acid phosphatase-1, one of the many acid phosphatases present in tomato (Lycopersicon esculentum Mill.

Cited by 46 publications

References 13 publications

Methyl jasmonate inhibition of root growth and induction of a leaf protein are decreased in an Arabidopsis thaliana mutant.

Methyl jasmonate inhibition of root growth and induction of a leaf protein are decreased in an Arabidopsis thaliana mutant.

Arabidopsis Vegetative Storage Protein Is an Anti-Insect Acid Phosphatase

Isolation and partial characterisation of acid phosphatase isozymes from dormant oilseed of Corylus avellana L.

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