Ectopic Expression of a Phytase Gene from <i>Medicago truncatula</i> Barrel Medic Enhances Phosphorus Absorption in Plants

Xiao, Kai; Zhang, Jianheng; Harrison, Maria J.; Wang, Zeng‐Yu

doi:10.1111/j.1744-7909.2006.00189.x

Cited by 7 publications

(5 citation statements)

References 32 publications

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“…2003), MtPHY1 of Medicago truncatula (Xiao et al . 2005, 2006b), and MtPAP1 of Medicago truncatula (Xiao et al . 2006a).…”

Section: Introductionmentioning

confidence: 99%

“…The mobility of phosphorus (P) in soil is very low, therefore, the efficiency of the use of P in soil as a fertilizer is low. The P in soil exists mostly in unavailable forms, such as organic P and insoluble inorganic P. To improve the efficiency of P acquisition from the soil, many attempts to improve the ability of plants to utilize organic P have been conducted using genetic modification (George et al 2004, 2005c, Lung et al 2005Mudge et al 2003;Richardson et al 2001;Xiao et al 2005Xiao et al , 2006aYip et al 2003;Zimmernann et al 2003). Phytate (inositol hexakisphosphate) is the most abundant organic P in soil (Turner et al 2002); thus, improvement in phytate hydrolyzing activity has been the major focus of many studies.…”

Section: Introductionmentioning

confidence: 99%

“…Phytate (inositol hexakisphosphate) is the most abundant organic P in soil (Turner et al 2002); thus, improvement in phytate hydrolyzing activity has been the major focus of many studies. The utilization of phytate-P, existing as a soluble form, can be improved by the introduction of phytases and an acid phosphatase (APase), such as phyA of Aspergillus niger (George et al 2004(George et al , 2005cMudge et al 2003;Richardson et al 2001), 168phyA of Bacillus subtilis (Yip et al 2003), a synthetic gene for secretory phytase (Zimmernann et al 2003), MtPHY1 of Medicago truncatula (Xiao et al 2005(Xiao et al , 2006b, and MtPAP1 of Medicago truncatula (Xiao et al 2006a). For example, P acquisition from soluble phytate in agar media by transgenic Arabidopsis and subterranean clover with ex::phyA, a chimeric phytase gene of Aspergillus niger with a signal peptide of carrot extensin required for extracellular proteins, was better than that by wild-type plants (George et al 2004;Richardson et al 2001).…”

Section: Introductionmentioning

confidence: 99%

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Overexpression of theLASAP2gene for secretory acid phosphatase in white lupin improves the phosphorus uptake and growth of tobacco plants

Wasaki¹,

Maruyama

Tanaka

et al. 2009

Soil Science and Plant Nutrition

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Secretion of acid phosphatase (APase) from the roots to take up phosphorus (P) is a well-known strategy of plants under P-deficient conditions. White lupin, which shows vigorous growth in low-P soils, is noted for its ability to secrete APase under P-deficient conditions. The APase secreted by white lupin roots is stable in soil solution and shows low substrate specificity, suggesting that genetic modification of plants using the APase gene LASAP2 might improve their ability to use organic P. The objective of the present study was to evaluate the potential of LASAP2 transgenic plants to increase organic P utilization. Dry matter production and P accumulation were higher in LASAP2 transgenic tobacco plants grown in gel media containing soluble phytate as the sole P source than in wild-type tobacco plants. Phosphorus uptake by the transgenic plants also increased in soil culture conditions. LASAP2 was apparently more effective in the liberation of organic P, including phytate, in the soil than the native tobacco APase. Thus, the enzymatic stability of LASAP2 in the soil appears to be an important factor for P acquisition.

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“…2003), MtPHY1 of Medicago truncatula (Xiao et al . 2005, 2006b), and MtPAP1 of Medicago truncatula (Xiao et al . 2006a).…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Overexpression of theLASAP2gene for secretory acid phosphatase in white lupin improves the phosphorus uptake and growth of tobacco plants

Wasaki¹,

Maruyama

Tanaka

et al. 2009

Soil Science and Plant Nutrition

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“…A third phytase gene ( GmPhy ) has been isolated from soybean ( Glycine max ), and is expressed in the cotyledons of germinating soybean seedlings (Hegeman and Grabau, 2001). The Medicago truncatula L. MtPAP1 and MtPhy1 phytase genes have been isolated, and have been found to be expressed in the leaf, stem and roots of the developing plant (Xiong et al ., 2004; Xiao et al ., 2006). The M. truncatula and soybean phytases all belong to the PAP group, whereas the maize phytases are HAPs.…”

Section: Introductionmentioning

confidence: 99%

Wheat (Triticum aestivum L.) and barley (Hordeum vulgare L.) multiple inositol polyphosphate phosphatases (MINPPs) are phytases expressed during grain filling and germination†

Dionisio

Holm

Brinch-Pedersen³

2007

Plant Biotechnology Journal

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SummaryAt present, little is known about the phytases of plant seeds in spite of the fact that this group of enzymes is the primary determinant for the utilization of the major phosphate storage compound in seeds, phytic acid. We report the cloning and characterization of complementary DNAs (cDNAs) encoding one of the groups of enzymes with phytase activity, the multiple inositol phosphate phosphatases (MINPPs). Four wheat cDNAs ( TaPhyIIa1 , TaPhyIIa2 , TaPhyIIb and TaPhyIIc ) and three barley cDNAs ( HvPhyIIa1 , HvPhyIIa2and HvPhyIIb ) were isolated. The open reading frames ranged from 1548 to 1554 bp and the level of homology between the barley and wheat proteins ranged from 90.5% to 91.9%. All cDNAs contained an N-terminal signal peptide encoding sequence, and a KDEL-like sequence, KTEL, was present at the C-terminal, indicating that the enzyme was targeted to and retained within the endoplasmic reticulum. Expression of TaPhyIIa2 and HvPhyIIb in Escherichia coli revealed that the MINPPs possessed a significant phytase activity with narrow substrate specificity for phytate. The pH and temperature optima for both enzymes were pH 4.5 and 65 ° C, respectively, and the K m values for phytate were 246 and 334 µ M for the wheat and barley recombinant enzymes, respectively. The enzymes were inhibited by several metal ions, in particular copper and zinc. The cDNAs showed significantly different temporal and tissue-specific expression patterns during seed development and germination. With the exception of TaPhyIIb , the cDNAs were present during late seed development and germination. We conclude that MINPPs constitute a significant part of the endogenous phytase potential of the developing and germinating barley and wheat seeds.

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“…5) indicated that a single gene encoding the VrPAP1 is present in mungbean genome. In Medicago truncatula genome, two copies of PAP (Xiao et al 2006a) and PAP phytase (Xiao et al 2006b) genes exist whereas at least 2 -3 copies of NtPAP4, NtPAP12, NtPAP19, and NtPAP21 genes (Kaida et al 2003) are present in the Nicotiana tabacum genome. The results obtained in this study show that VrPAP1 belongs to the purple acid phosphatase family.…”

Section: T-m-p; and 4) D-c-y-s-c-(s/amentioning

confidence: 99%

Isolation and characterization of purple acid phosphatase gene during seedling development in mungbean

Wongkaew¹,

Srinives²,

Nakasathien³

2013

Biologia plant.

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Purple acid phosphatases (PAPs), which are normally found in plant tissues, can hydrolyze a broad spectrum of phosphate esters. In this study, a mungbean [Vigna radiata (L.) Wilczek cv. KPS1] acid phosphatase gene (VrPAP1) was isolated from seedling cotyledons. The full-length of VrPAP1 cDNA contained an open reading frame of 1 644 bp encoding 547 amino acid residues with a predicted molecular mass of 62.07 kDa. Sequence analysis showed that VrPAP1 is purple acid phosphatase. RNA blot analyses indicated that the VrPAP1 accumulated during the first hour in cotyledons of germinating seeds and reached a maximum expression after 24 h and then decreased. The VrPAP1 mRNA was observed in cotyledons, hypocotyls and leaves but not in radicles or dry seeds. DNA blot analysis indicated that VrPAP1 is a single copy gene in the mungbean genome.

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Ectopic Expression of a Phytase Gene from Medicago truncatula Barrel Medic Enhances Phosphorus Absorption in Plants

Cited by 7 publications

References 32 publications

Overexpression of theLASAP2gene for secretory acid phosphatase in white lupin improves the phosphorus uptake and growth of tobacco plants

Overexpression of theLASAP2gene for secretory acid phosphatase in white lupin improves the phosphorus uptake and growth of tobacco plants

Wheat (Triticum aestivum L.) and barley (Hordeum vulgare L.) multiple inositol polyphosphate phosphatases (MINPPs) are phytases expressed during grain filling and germination†

Isolation and characterization of purple acid phosphatase gene during seedling development in mungbean

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