A phosphate starvation-induced acid phosphatase from Oryza sativa: phosphate regulation and transgenic expression

Hur, Yeon Jae; Lee, Han Gil; Jeon, Eun Ji; Lee, Yun Young; Nam, Min Hee; Yi, Gihwan; Eun, Moo Young; Nam, Jaesung; Lee, Jai Heon; Kim, Doh Hoon

doi:10.1007/s10529-007-9318-5

Cited by 27 publications

(15 citation statements)

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“…Several studies have reported that overexpression of secreted PAPs can improve plant biomass and Pi accumulation (Xiao et al, 2006;Hur et al, 2007;Ma et al, 2009;Wang et al, 2009). However, these attempts have either focused around high-specificity phytases or PAPs with extracellular roles, but unclear intracellular function.…”

Section: Resultsmentioning

confidence: 99%

The Dual-Targeted Purple Acid Phosphatase Isozyme AtPAP26 Is Essential for Efficient Acclimation of Arabidopsis to Nutritional Phosphate Deprivation

et al. 2010

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Induction of intracellular and secreted acid phosphatases (APases) is a widespread response of orthophosphate (Pi)-starved (2Pi) plants. APases catalyze Pi hydrolysis from a broad range of phosphomonoesters at an acidic pH. The largest class of nonspecific plant APases is comprised of the purple APases (PAPs). Although the biochemical properties, subcellular location, and expression of several plant PAPs have been described, their physiological functions have not been fully resolved. Recent biochemical studies indicated that AtPAP26, one of 29 PAPs encoded by the Arabidopsis (Arabidopsis thaliana) genome, is the predominant intracellular APase, as well as a major secreted APase isozyme up-regulated by 2Pi Arabidopsis. An atpap26 T-DNA insertion mutant lacking AtPAP26 transcripts and 55-kD immunoreactive AtPAP26 polypeptides exhibited: (1) 9-and 5-fold lower shoot and root APase activity, respectively, which did not change in response to Pi starvation, (2) a 40% decrease in secreted APase activity during Pi deprivation, (3) 35% and 50% reductions in free and total Pi concentration, respectively, as well as 5-fold higher anthocyanin levels in shoots of soil-grown 2Pi plants, and (4) impaired shoot and root development when subjected to Pi deficiency. By contrast, no deleterious influence of AtPAP26 loss of function occurred under Pi-replete conditions, or during nitrogen or potassium-limited growth, or oxidative stress. Transient expression of AtPAP26-mCherry in Arabidopsis suspension cells verified that AtPAP26 is targeted to the cell vacuole. Our results confirm that AtPAP26 is a principal contributor to Pi stress-inducible APase activity, and that it plays an important role in the Pi metabolism of 2Pi Arabidopsis.Orthophosphate (Pi) is an essential plant macronutrient required for many pivotal metabolic processes such as photosynthesis and respiration. However, the massive use of Pi fertilizers in agriculture demonstrates how the free Pi level of many soils is suboptimal for plant growth. The world's reserves of rock phosphate, our major source of Pi fertilizers, are projected to be depleted by the end of this century (Vance et al., 2003). Furthermore, Pi runoff from fertilized fields into nearby surface waters results in environmentally destructive processes such as aquatic eutrophication and blooms of toxic cyanobacteria. Effective biotechnological strategies are needed to engineer Pi-efficient transgenic crops to ensure agricultural sustainability and a reduction in Pi fertilizer overuse. This necessitates a detailed understanding of Pi-starvation-inducible (PSI) gene expression and the complex morphological, physiological, and biochemical adaptations of Pi-deficient (2Pi) plants.A well-documented component of the plant Pi stress response is the up-regulation of intracellular and secreted acid phosphatases (APases; E.C. 3.1.3.2) that catalyze the hydrolysis of Pi from various phosphate monoesters and anhydrides in the acidic pH range (Tran et al., 2010a). APase induction by 2Pi plants has been correlated wit...

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Section: Resultsmentioning

confidence: 99%

The Dual-Targeted Purple Acid Phosphatase Isozyme AtPAP26 Is Essential for Efficient Acclimation of Arabidopsis to Nutritional Phosphate Deprivation

et al. 2010

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“…APases catalyze the cleavage of Pi from phosphate esters under acidic conditions. Both intracellular and secreted APases are induced during Pi deficiency (Baldwin et al 2001;Hur et al 2007;Wang et al 2014). Intracellular APases are involved in recycling and remobilizing Pi from senescent tissue, while secreted APases are involved in scavenging of Pi from organic sources in the external environment (Robinson et al 2012a, b;Tian et al 2012;Vance et al 2003).…”

Section: Introductionmentioning

confidence: 99%

“…Purple acid phosphatases (PAPs) form a unique group among the APases, characterized by the purple color of the purified protein in aqueous solution and an iron (III)-containing dimetal center in the catalytic site (Olczak et al 2003;Strater et al 1995). PAPs have been found in, and characterized from, many plant species, including Arabidopsis, rice, tobacco, sweet potato, kidney bean and soybean, as well as other crop plants (Dionisio et al 2011;Durmus et al 1999;Hur et al 2007;Kaida et al 2003;Li et al 2002;Liang et al 2012;Liang 1998;Schenk et al 1999). PAPs contain five conserved amino acid motifs required for metal binding: DXG/GDXXY/GNH[D/E]/VXXH/ GHXH (bold letters represent the metal-binding residues) (Li et al 2002;Schenk et al 2000;Strater et al 1995).…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization of a tomato purple acid phosphatase during seed germination and seedling growth under phosphate stress

2015

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SlPAP1 is a phosphate starvation responsive purple acid phosphatase during tomato seed germination. Future research on its family members in tomato might improve the phosphate stress tolerance. Phosphate deficiency is a major constraint upon crop growth and yield. In response to phosphate deficiency, plants secrete acid phosphatases (APases) to scavenge organic phosphate from soil. In this study, we investigated the impact of Pi starvation on germination and seedling growth of tomato, and we then cloned and characterized a phosphate starvation responsive purple APase (SlPAP1) that expressed during tomato seedling growth. Our results showed that phosphate deficiency reduced germination and growth rates of tomato, and also increased intracellular and secretory APase activity in a concentration-dependent manner. An in-gel activity assay found that two APases of 50 and 75 kDa were secreted during conditions of phosphate deficiency. SlPAP1 is a single copy gene belonging to a small gene family. It was expressed as a cDNA of approximately 1.5 kbp encoding a secreted glycoprotein of 470 amino acids. Northern blot analysis showed that SlPAP1 was specifically expressed in root tissue during phosphate deficiency. SlPAP1 had high sequence identity (56-89%) with other plant PAPs and contained highly conserved metal-binding residues. SlPAP1 is the first PAP to be cloned and characterized from tomato. This study provides useful information for future research on PAP family members in tomato, leading to better understanding of phosphate deficiency in this important crop plant.

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“…On the other hand, our recent results indicated that rice acid phosphatase (OsACP1) is up-regulated specifically during P i starvation and is functionally expressed in transgenic Arabidopsis. This finding suggests that the OsACP1 gene can be used to develop new transgenic dicotyledonous plants that are able to adapt to P i -deficient conditions (Hur et al 2007).…”

Section: Introductionmentioning

confidence: 93%

Molecular characterization of OsPAP2: transgenic expression of a purple acid phosphatase up-regulated in phosphate-deprived rice suspension cells

et al. 2009

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A phosphate starvation-induced, purple, acid phosphatase cDNA was cloned from rice, Oryza sativa. The cDNA encoding the phosphatase (OsPAP2) has 1,893 bp with an open reading frame of 630 amino acid residues. The deduced amino acid sequence of OsPAP2 shows identities of 60-63% with other plant purple acid phosphatases and appears to have five conserved motifs containing the residues involved in metal binding. OsPAP2 expression is up-regulated in the rice plant and in cell cultures in the absence of phosphate (P( i )). The induced expression of OsPAP2 is a specific response to P( i ) starvation, and is not affected by the deprivation of other nutrients. OsPAP2 expression was responsive to the level of P( i )-supply, and transcripts of OsPAP2 were abundant in P( i )-deprived roots. The OsPAP2 cDNA was expressed as a 69 kDa polypeptide in baculovirus-infected insect Sf9 cells. In addition, the OsPAP2 gene was introduced into Arabidopsis via an Agrobacterium-mediated transformation. Functional expression of the OsPAP2 gene in the transgenic Arabidopsis line was confirmed by northern and western blot analyses, as well as by phosphatase activity assays. These results suggest that the OsPAP2 gene can be used to develop new transgenic dicotyledonous plants that are able to adapt to P( i )-deficient conditions.

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A phosphate starvation-induced acid phosphatase from Oryza sativa: phosphate regulation and transgenic expression

Cited by 27 publications

References 14 publications

The Dual-Targeted Purple Acid Phosphatase Isozyme AtPAP26 Is Essential for Efficient Acclimation of Arabidopsis to Nutritional Phosphate Deprivation

The Dual-Targeted Purple Acid Phosphatase Isozyme AtPAP26 Is Essential for Efficient Acclimation of Arabidopsis to Nutritional Phosphate Deprivation

Molecular characterization of a tomato purple acid phosphatase during seed germination and seedling growth under phosphate stress

Molecular characterization of OsPAP2: transgenic expression of a purple acid phosphatase up-regulated in phosphate-deprived rice suspension cells

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