Isolation and Characterization of a Tomato Acid Phosphatase Complementary DNA Associated with Nematode Resistance

Erion, Jack L.; Ballo, Barbara; May, Lisa; Bussell, John D.; Fox, Tim W.; Thomas, Steve

doi:10.1104/pp.97.4.1462

Cited by 7 publications

(5 citation statements)

References 23 publications

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“…The first plant gene to be classified as an ACP was from tomato, although interest in it was primarily due to its tight genetic linkage to a root-knot nematode-resistance gene rather than to its enzymic activity (Aarts et al, 1991;Erion et al, 1991;Williamson and Colwell, 1991). The other plant AP that has been cloned and sequenced is the soybean VSP (Staswick 1988;Dewald et al, 1992), which has been shown to possess some phosphatase activity (Dewald et al, 1992).…”

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confidence: 99%

Soybean Root Nodule Acid Phosphatase

1997

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Acid phosphatases are ubiquitous enzymes that exhibit activity against a variety of substrates in vitro, although little is known about their intracellular function. In this study we report the isolation, characterization, and partia1 sequence of the major acid phosphatase from soybean (Clycine max 1.) root nodules. l h e phosphatase was purified predominantly as a heterodimer with subunits of 28 and 31 kD; homodimers of both subunits were also observed and exhibited phosphatase activity. In addition to the general phosphatase substrate, pnitrophenyl phosphate, the heterodimeric form of the enzyme readily hydrolyzed 5'-nucleotides, flavin mononucleotide, and O-phospho-L-Tyr. Low or negligible activity was observed with ATP or polyphosphate. Purified nodule acid phosphatase was stimulated by magnesium, inhibited by calcium and EDTA, and competitively inhibited by cGMP and cAMP with apparent Ki values of 7 and 1 2 PM, respectively. Partia1 N-terminal and interna1 sequencing of the nodule acid phosphatase revealed homology to the soybean vegetative storage proteins. There was a 17-fold increase in enzyme activity and a noticeable increase in protein levels detected by immunoblotting methods during nodule development. Both of these parameters were low in young nodules and reached a peak in mature, functional nodules, suggesting that this enzyme is important for efficient nodule metabolism.General phosphohydrolases are classified as alkaline phosphatases or acids based solely upon whether their optimal activity is above or below pH 7.0 (Vincent et al., 1992). Whereas plant alkaline phosphatases have been characterized as having specific metabolic roles, most plant ACPs have been shown to hydrolyze a wide variety of phosphorylated substrates in vitro, making their cellular role(s) difficult to define (for review, see Duff et al. [1994]). One method of determining the substrate specificity of an ACP is to determine the kinetic parameters of specificity such as V,,,lK, with numerous substrates. This approach was taken by Duff et al. (1989aDuff et al. ( , 1989bDuff et al. ( , 1991 to characterize an ACP from Brassica nigra suspension-cultured cells as a PEP phosphatase.The difficulty in classifying plant ACPs is further compounded by a lack of available sequence information: Only

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confidence: 99%

Soybean Root Nodule Acid Phosphatase

1997

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“…These sequences shared 64, 56, and 54% identity, respectively. The LASAP1 sequence, however, had no significant homology with other types of APases, such as tomato APSl (Aarts et al 1991;Erion et al 1991Erion et al , 1992Williamson and Colwell 1991;Tanaka et al 1992). In KBPAP, 7 metal-binding sites and a general active site have been identified from the crystal structure (Strater et al 1995).…”

Section: Resultsmentioning

confidence: 94%

Structure of a cDNA for an acid phosphatase from phosphate-deficient lupin (Lupinus albusL.) Roots

Wasaki

Omura

Osaki

et al. 1999

Soil Science and Plant Nutrition

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“…The deduced amino acid sequence of the PSP cDNA was found to have 71 and 65% identity with those of VSP-LU and VSP-p of soybean, respectively (Rhee and Staswick, 1992a, 199213). PSP also had 40% sequence identity with tomato acid phosphatase-1 (Erion et al, 1991). The amino acid sequences of acid phosphatase-1 and VSP share about 45% identity.…”

Section: Cenomic Southern Blot Analysismentioning

confidence: 92%

“…The N-terminal amino acid sequence of forms A and C of PSP corresponded to amino acid residues 37 to 52. The deduced amino acid sequence of the APSP1 cDNA has 71 and 65% identity with those of VSP-a and VSP-/3 of soybean, respectively Staswick, 1992a, 1992b), and 40% identity with acid phosphatase-1 of tomato (Erion et al, 1991). No putative glycosylation sites were contained in the deduced amino acid sequence of APSP1 cDNA (Fig.…”

Section: Nucleotide Sequence Of Psp Cdnamentioning

confidence: 98%

“…PSP cDNA clones were isolated, and the deduced amino acid sequence showed 65 to 71% identity with the sequences of VSPs from soybean (Glycine man) leaves (Staswick, 1988) and 40% identity with the sequences of acid phosphatase-1 from tomato (Erion et al, 1991). (Pkaseolus vul-garis) plants, the accumulation of protein in developing pods precedes that in se& (Endo et al, 1987).…”

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A 28-Kilodalton Pod Storage Protein of French Bean Plants (Purification, Characterization, and Primary Structure)

et al. 1997

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When French bean (Pbaseolus vulgaris) plants were depodded in the early stages of fruit development, relative levels of a specific protein with a relative molecular weight of 28,000 were enhanced in the young pods that formed later. The protein, designated pod storage protein (PSP), was purified from extracts of newly formed pods from plants that had been previously depodded four times at intervals of 2 weeks. Two-dimensional polyacrylamide gel electrophoresis showed the presence of three forms (designated A, B, and C) of PSP with identical electrophoretic mobilities but different charges. The molecular mass of native PSP was estimated by gel filtration t o be 67 kD; therefore, the protein was most likely present as a dimer. The antisera raised against forms A and C were cross- mobilization in pods during fruit maturation (Tanaka et al., 1993).In the course of studies of endopeptidases in pods of French bean plants, we found that when a large number of pods in the early stages of fruit development were removed from a plant, relative levels of a specific protein with an M, of 28,000 were enhanced in the newly formed pods. The protein accumulated to high levels in the pods of plants that had been previously depodded, whereas a smaller amount was detected in the pods of nontreated plants. It was postulated that enhanced levels of the M, 28,000 protein resulted from a reduction of plant sink size caused by removing pods in the early stages of fruit development.In this report, we characterize this protein from French bean pods and designate it PSP. PSP cDNA clones were isolated, and the deduced amino acid sequence showed 65 to 71% identity with the sequences of VSPs from soybean (Glycine man) leaves (Staswick, 1988) and 40% identity with the sequences of acid phosphatase-1 from tomato (Erion et al., 1991). (Pkaseolus vul-garis) plants, the accumulation of protein in developing pods precedes that in se& (Endo et al., 1987). As reported for other legumes such as field pea (Flinn and Pate, 1968), bean (Oliker, 1978), and cowpea (Peoples et al., 1985a(Peoples et al., , 1985b(Peoples et al., , 1985c, protein accumulates in French bean seeds during fruit development concurrently with active mobilization of protein and free amino acids in the pods. Thus, a proportion of seed nitrogen is temporarily stored in pods Dry seeds of French bean (Phaseolus vulgaris L. cv Goldchased from Sakata Seed (Yokohamat Japan). If stated with 13 h of light (190 p E s-l m-') and 11 h of darkness at 25°C and, at desired developmental stages, maturing fruits were harvested and stored at -20°C until use. For the purification of PSP, pods were collected as follows: just star) and "ybean (Glycine max cv Mikawajima) were purOtherwise, MATERIALS AND METHODS During fruit development in French beanFrench bean plants were grown in a phytotron as proteins, amino acids, and probably small peptides, which are then mobilized to support the growth of seeds.activity throughout the development and subsequent senescence of French bean pods (Endo et al., 1987)....

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Isolation and Characterization of a Tomato Acid Phosphatase Complementary DNA Associated with Nematode Resistance

Cited by 7 publications

References 23 publications

Soybean Root Nodule Acid Phosphatase

Soybean Root Nodule Acid Phosphatase

Structure of a cDNA for an acid phosphatase from phosphate-deficient lupin (Lupinus albusL.) Roots

A 28-Kilodalton Pod Storage Protein of French Bean Plants (Purification, Characterization, and Primary Structure)

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