Identification of soybean purple acid phosphatase genes and their expression responses to phosphorus availability and symbiosis

Li, Chengchen; Gui, Shun‐Hua; Yang, Tao; Walk, Thomas C.; Wang, Xiurong; Liao, Hong

doi:10.1093/aob/mcr246

Cited by 136 publications

(124 citation statements)

References 51 publications

Supporting

Mentioning

118

Contrasting

Order By: Relevance

“…Plant APases are classified in five distinct families (Feizi & Malboobi unpublished data), out of which purple acid phosphatases (PAPs) form the largest clade. For example, Arabidopsis, rice and soybean genomes encompass 29, 26 and 35 PAP family members, respectively (Li et al 2002(Li et al , 2012Zhang et al 2011).…”

Section: −mentioning

confidence: 99%

Improved phosphate metabolism and biomass production by overexpression of AtPAP18 in tobacco

et al. 2012

View full text Add to dashboard Cite

Limited availability of phosphate ion (Pi) reduces plant growth in natural ecosystems. Here, we report the functional effects of overexpressing an Arabidopsis thaliana purple acid phosphatase encoding gene, AtPAP18, in Nicotiana tabbacum as a crop model plant. Transgenic tobacco plants exhibited significant increases in acid phosphatase activity, total P and Pi contents leading to improved biomass production in both Pi-deficient and Pi-sufficient conditions. Transient expression of AtPAP18::green fluorescent fusion protein in onion epidermal cells indicated that AtPAP18 is a dual-targeted protein, which is detected mainly in the apoplast of the cells after 24 h and in the vacuole after 72 h. Possibly, AtPAP18 protein confers efficient retrieval of Pi from bonded extracellular compounds as well as expendable intracellular Pi-monoesters and anhydrides. These data clearly indicate that overexpression of AtPAP18 gene offers an effective approach for reducing the consumption of chemical Pi fertilizer through increased acquisition of soil Pi and mobilization of internal resources.

show abstract

Section: −mentioning

confidence: 99%

Improved phosphate metabolism and biomass production by overexpression of AtPAP18 in tobacco

et al. 2012

View full text Add to dashboard Cite

show abstract

“…The increase in phosphatase activity has been attributed to synthesis of enzymes of the same type or to the activation of preexisting acid phosphatases (Wasaki et al, 2009;Tran et al, 2010;Li et al, 2011).…”

Section: Detection Of Acid Phosphatase Isoenzymes In Ectomycorrhizal mentioning

confidence: 99%

“…Among these factors, inorganic phosphorous is probably the most important in vivo repression of phosphatase synthesis (van Aarle & Plassard, 2010;Tran et al, 2010;Li et al, 2011). Deficiency or absence of phosphate in the culture medium leads to a significant increase in activity of acid phosphatases in ectomycorrhizal fungi (Tibbett et al, 1998;Tran et al, 2010;Bechem, 2013).…”

Section: Introductionmentioning

confidence: 99%

“…Deficiency or absence of phosphate in the culture medium leads to a significant increase in activity of acid phosphatases in ectomycorrhizal fungi (Tibbett et al, 1998;Tran et al, 2010;Bechem, 2013). This increase in activity results from the normal secretion of surface phosphatases and liberation of extracellular phosphatases (Alvarez et al, 2005;Tran et al, 2010) leading to a more efficient utilization of different forms of organic phosphorous (Wang et al, 2006;Khade et al, 2010), thereby contributing to the nutrition of infected plants (Stancheva et al, 2008;Wu et al, 2011;Li et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

“…The increase in synthesis or activity of acid phosphatases may be due to the synthesis of new inducible isoenzymes localized in the cell wall or the external face of the plasma membrane (Pasqualini et al, 1992), or to the activation of preexisting molecules (Berjaud & D'Auzac, 1986;Playsted et al, 2006;Wasaki et al, 2009;Tran et al, 2010;Li et al, 2011). It is suggested, therefore, that the increasing in acid phosphatase activity in P. microcarpus RV82, when grown in medium without phosphate or with low concentrations of inorganic phosphate may be partly due to the production of new types of isoenzymes.…”

mentioning

confidence: 99%

See 2 more Smart Citations

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

Biological and Biomedical Aspects of Metal Phenolates

Ming

2014

Patai's Chemistry of Functional Groups

View full text Add to dashboard Cite

The phenol functionality is involved in diverse biological processes and functions, serving as a proton donor and as a metal‐binding ligand. It is commonly found in many biochemicals (such as siderophores and the amino acids tyrosine and tryptophan), pharmaceuticals (including antibiotics, metal‐chelating agents, and diagnostic agents), and natural products (such as polyphenols, flavonoids, and salicylic acid). In association with other functional groups, the phenol moiety forms various types of metal‐binding sites of diverse structures and functions, for example, for iron binding and transport, in enzymes for oxygenation of substrates, and for biotransformation of aromatic compounds. Many environmentally hazardous aromatic compounds such as bisphenol A, PCB, and DDT can be degraded by tyrosinate(phenolate)‐containing metalloenzymes from microorganisms, which provides a clue for bioremediation of these toxic substances. Moreover, the phenol‐containing wet‐adhesive byssal proteins from some clams and mussels has stimulated further development of adhesive materials for medical and other applications; and the study of binding of transferrin with nanoparticles affords better understanding of protein–mineral interfacial interactions. In addition to these naturally occurring metal‐phenolate centers, there are many metal complexes of phenol and derivatives that exhibit various catalytic activities and serve as structural and/or functional model systems for tyrosinate‐containing metalloproteins.

show abstract

Identification of soybean purple acid phosphatase genes and their expression responses to phosphorus availability and symbiosis

Cited by 136 publications

References 51 publications

Improved phosphate metabolism and biomass production by overexpression of AtPAP18 in tobacco

Improved phosphate metabolism and biomass production by overexpression of AtPAP18 in tobacco

Activity of Acid Phosphatases in Ectomycorrhizal Fungi

Biological and Biomedical Aspects of Metal Phenolates

Contact Info

Product

Resources

About