Feeding hungry plants: The role of purple acid phosphatases in phosphate nutrition

Tran, Hue T.; Hurley, Brenden A.; Plaxton, William C.

doi:10.1016/j.plantsci.2010.04.005

Cited by 234 publications

(277 citation statements)

References 96 publications

Supporting

Mentioning

270

Contrasting

Unclassified

Order By: Relevance

“…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 with de novo APase synthesis in several species, including white lupin (Lupinus albus), tomato (Solanum lycopersicum), and Arabidopsis (Arabidopsis thaliana ;Miller et al, 2001;Bozzo et al, 2006;Veljanovski et al, 2006;Bozzo and Plaxton, 2008;Tran and Plaxton, 2008).…”

mentioning

confidence: 99%

“…The probable function of intracellular APases is to recycle Pi from expendable intracel-lular organophosphate pools. This is accompanied by a marked reduction in cytoplasmic phosphate metabolites during extended Pi stress (Bozzo and Plaxton, 2008;Tran et al, 2010a). Secreted APases belong to a group of PSI phosphohydrolases believed to mobilize Pi from the external organophosphates prevalent in many soils (Vance et al, 2003;Bozzo and Plaxton, 2008).…”

mentioning

confidence: 99%

See 1 more Smart Citation

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

et al. 2010

Self Cite

View full text Add to dashboard Cite

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...

show abstract

mentioning

confidence: 99%

mentioning

confidence: 99%

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

et al. 2010

Self Cite

View full text Add to dashboard Cite

show abstract

“…Acid phosphatases predominate in acid soils (Tran et al, 2010) and fungi generally present higher activities of these phosphatases (van Aarle & Plassard, 2010). Intra and interspecific differences in phosphatase activities have been observed in ectomycorrhizal fungi (Sawyer et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

“…Intra and interspecific differences in phosphatase activities have been observed in ectomycorrhizal fungi (Sawyer et al, 2003). Factors such as pH (Alvarez et al, 2005), fungal growth rate and temperature (Chethan Kumar et al, 2008), mycelial age (Nygren & Rosling, 2009), water stress (Wu et al, 2011) mycorrhizal colonization (Stancheva et al, 2008;Wu et al, 2011) and phosphorous source and concentration (Nygren & Rosling, 2009;van Aarle & Plassard, 2010;Tran et al, 2010;Bechem, 2013) all influence acid phosphatase activity.…”

Section: Introductionmentioning

confidence: 99%

Activity of Acid Phosphatases in Ectomycorrhizal Fungi

Costa¹,

Souza²,

Rondon³

et al. 2016

JAS

View full text Add to dashboard Cite

The colonization of plant roots by mycorrhizal fungi, generally increases P content in the host plant when in soils with low levels of P. The objective of this work was to evaluate the activity of acid phosphatases in two isolates of Pisolithus microcarpus, grown in different sources and concentrations of phosphate and to characterize the phosphatase isoenzymes produced by isolates. Both isolates were grown on Melin-Norkrans modified (MNM) medium enriched with organic (Po) or inorganic (Pi) sources of phosphorus, at five different concentrations, in order to study the activity of mycelial surface acid phosphatases during incubation for up to 96 h. Activity of acid phosphatases increased when the fungi were grown without or at low concentrations of Pi. Intraspecific differences were observed between the isolates with regard to acid phosphatase production. A greater decrease in phosphatase activity was observed when incubation time was increased than when Pi concentration was increased. At an incubation time of 96 h, activity of acid phosphatases in isolate 90A increased with increasing Po concentration, while for isolate RV82 remained constant over the different incubation periods and Po concentrations tested. When grown in media without Pi, an additional band appeared in the isoenzyme pattern of RV82, while isoenzyme production was not altered in isolate 90A when grown in media without Pi or with 2 mM Pi, showing differences in their isoenzyme patterns. Isolate 90A possesses a potential competitive advantage when utilized in mycorrhizal association with Eucalyptus because of its ability to utilize Po.

show abstract

“…82,114-116,119-121,123 Nonetheless, they are postulated to participate in mobilising inorganic phosphate in the soil during seed germination. 49,77,[114][115][116]128,[149][150] As well as their function as phosphatases, mammalian PAPs play a role in iron transport during pregnancy, 151 and macrophage-specific generation of reactive oxygen species (ROS) in response to pathogen invasion of hosts. 152 ROS generation is believed to be of the iron catalysed Haber/WeissFenton reactions (equations 2 and 3) by the redox-active diiron centre in mammalian PAPs, as was shown in vitro.…”

Section: Paps' Biological Functionsmentioning

confidence: 99%

Design, synthesis and testing of purple acid phosphatase inhibitors for the development of anti-osteoporotic drugs

Pahmi¹

View full text Add to dashboard Cite

Purple acid phosphatases (PAPs) are binuclear metallohydrolases that have been isolated from various mammals, plants, fungi and bacteria. They catalyse phosphoric ester hydrolysis under acidic to neutral conditions by utilising two closely spaced heterovalent metal ions in their active sites. In mammals, PAP activity is associated with bone resorption, which can lead to bone diseases such as osteoporosis. For instance, osteoporosis patients are observed to have elevated PAP serum levels.Furthermore, research has shown that transgenic mice that over-expressed the PAP gene developed mild osteoporosis. These observations therefore make human PAP an attractive target to develop anti-osteoporotic drugs.This project employed the strategy of using a substrate analogue, where the lead compound (as shown below) with K i value of 8 µM against pig PAP was chosen as the basis in this rational drug design. Therefore acyl derivatives of α-aminoarylmethylphosphonic acids (as shown below) were designed as potential new potent PAP inhibitors. Docking studies suggested that the derivatives would have high binding affinity due to the phosphonate moiety (substrate mimic) binding to the binuclear metal centre, which are as intended. Furthermore, the long acyl chains make favourable interactions with the long hydrophobic groove adjacent to the dimetal centre, and depending on the size and substitutions on the aromatic ring, the ring might occupy the space in any of the small pockets in the vicinity of the active site; all of which contribute to the predicted high binding affinities of the derivatives to the enzyme.The lead compound: (naphthalene-1-yl(tetradecanamido)methyl)phosphonic acidR 2 = Me(CH 2 ) m -, Me(CH 2 ) n OCH 2 -; m = 8, 10, 12, 14, 16; n = 7, 15, 17. Acyl derivatives of α-(amino(aryl)methyl)phosphonic acids IIIThe derivatives were synthesised in three or four steps method in good yields and then tested as pig PAP inhibitors. The kinetic studies in this project were performed using newly extracted and purified pig PAP. The extraction and purification of pig PAP from the allantoic fluid of a pregnant pig was successfully carried out using fast protein liquid chromatography (FPLC) by adapting a well-established protocol. Kinetic analysis showed that the derivatives have high inhibition potencies against pig PAP with K i values in the low micromolar to nanomolar range. The most potent pig PAP inhibitor within this series was the octadecyl-derivative of α-(phenyl(amido)methyl)phosphonic acid with K i value of 168 nM. This is the most potent pig PAP inhibitor to date.Screening tests on a hundred other compounds were also performed to identify new possible alternative PAP inhibitors. Most of the compounds have metal-binding moieties as they were developed as inhibitors of a metallo-β-lactamase, which is also a binuclear metallohydrolase.Therefore it was thought that they might have inhibition properties against PAPs. However, they were found to have little or no inhibition against pig PAP. Nonetheless, these results ...

show abstract

Feeding hungry plants: The role of purple acid phosphatases in phosphate nutrition

Cited by 234 publications

References 96 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

Activity of Acid Phosphatases in Ectomycorrhizal Fungi

Design, synthesis and testing of purple acid phosphatase inhibitors for the development of anti-osteoporotic drugs

Contact Info

Product

Resources

About