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

Zamani, Katayoun; Sabet, Mohammad; Lohrasebi, Tahmineh; Mousavi, Amir; Malboobi, Mohammad Ali

doi:10.2478/s11756-012-0072-3

Cited by 15 publications

(15 citation statements)

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“…[49][50][51][52] Furthermore, having insighti nto the molecular details of the mechanism by whichp lant PAPs hydrolyze substrates will also contribute to the field of plant biotechnology,g uiding the designo ft ransgenic plants that express more efficient PAPs in ordert oi mprovec rop yields and reduce or eliminate the need for fertilizers. [53][54][55][56] …”

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The Binding Mode of an ADP Analogue to a Metallohydrolase Mimics the Likely Transition State

et al. 2019

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Purple acid phosphatases( PAPs) are members of the large family of metallohydrolases, ag roup of enzymes that perform aw ide range of biological functions, while employing ah ighly conserved catalytic mechanism. PAPs are found in plants,a nimals and fungi;i nh umans they play an important role in bone turnovera nd are thus of interest for developingt reatments for osteoporosis. The majority of metallohydrolases use am etalbound hydroxide to initiate catalysis, which leads to the formation of ap roposed five-coordinate oxyphosphorane species in the transition state. In this work, we crystallized PAPf rom red kidney beans (rkbPAP) in the presence of both adenosine and vanadate. The in crystallo-formed vanadate analogue of ADP provides detailed insight into the binding mode of aP AP substrate, captured in as tructure that mimics the putative fivecoordinate transition state. Our observations not only provide unprecedented insightinto the mechanism of metallohydrolases, but might also guide the structure-based design of inhibitors for application in the treatment of severalhuman illnesses.Metallohydrolases form al arge familyo fm ostly bimetallic enzymes that use metal ionst oactivate both the nucleophile and scissile bond of various phosphate or amide substrates. [1][2][3][4] Examples include the antibiotic-degrading metallo-b-lactamases, pesticide-decontaminating organophosphate hydrolases, and purple acid phosphatases (PAPs). [5][6][7] PAPs, the only known metallohydrolases that require ah eterovalent Fe III M II center (with M = Fe, Zn or Mn) for catalytic activity, have been characterized from various mammals, plants and fungi. [2,5] Mostp lant PAPs use either Zn II or Mn II ,w hereas their mammalianc ounterparts employ ar edox-activei ron ( Figure 1). [8,9] The reported substrates for PAPs include adenosine 5'-triphosphate (ATP), adenosine 5'-diphosphate( ADP), phosphotyrosine and pyrophosphate. [5,10] The synthetic substrate para-nitrophenyl phosphate (pNPP) is frequently used for functionalstudies. [2,5] The biological functions of PAPs are diverse and dependent on the organism. For mammals, experiments with transgenic mice have demonstrated that PAPp lays an important role in bone metabolism. [11,12] In plants, PAPs playamajor role in the acquisition of phosphorus, especially if there is al imited supplyo fp hosphate. [13,14] Due to their diverse roles, PAPs have attracted attention either as targetsf or new treatments of osteoporosis or for applicationsi na griculture to aid nutrient uptake by crops. [11,15] PAPs operate optimally in the pH range between5 .0 and 6.5, and are characterized by ad istinct purple color due to ac harge-transfer transition between an active-site tyrosine ligand and an Fe III ion. [16,17] The crystal structures of several mammalian and plant PAPs have demonstrated that, despite the difference in the metal ion selectivity and the limited degree of sequence similarity,t heir actives ite geometries are highly conserved (Figure1). [18][19][20][21][22][23] Consequently,t he proposed mod...

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The Binding Mode of an ADP Analogue to a Metallohydrolase Mimics the Likely Transition State

et al. 2019

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“…To determine the enzymatic activities, we constructed a standard curve using identified concentrations of PO 4 3 . We defined each unit of APase activity as 1 mmol of released Pi per min [13].…”

Section: Apase Activity Assaymentioning

confidence: 99%

“…Also, transgenic plants exhibited enhanced P efficiency and better root and shoot growth rates versus the controls [6]. Overexpression of AtPAP18 in Nicotiana tabbacum led to significantly increased acid phosphatase activity, total P and Pi contents, resulting in improved biomass production in both Pi-deficient and Pi-sufficient conditions [12,13].…”

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confidence: 99%

Agrobacterium rhizogenes transformed soybeans with AtPAP18 gene show enhanced phosphorus uptake and biomass production

Younessi-Hamzekhanlu

Izadi-Darbandi

Malboobi

et al. 2018

Biotechnology & Biotechnological Equipment

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Low-phosphorus stress is a challenging factor in limiting plant development. Soybean is cultivated in soils often low in phosphorus. However, on average 65% of total P is in the form of organic phosphates, which are unavailable to plants unless hydrolyzed to release inorganic phosphate. One approach for enhancing crop P acquisition from organic P sources is boosting the activity of acid phosphatases (APases). This study seeks to understand the role of an Arabidopsis (Arabidopsis thaliana) purple APase gene (AtPAP18) in soybean. Thus, the gene was isolated and a final vector (AtPAP18/pK7GWG2D) was built. Composite soybean plants were created using Agrobacterium rhizogenes-mediated transformation. A. rhizogenes K599 carrying the AtPAP18/pK7GWG2D vector with egfp as a reporter gene was used for soybean hairy root transformation. Analysis of Egfp expression detected fluorescence signals in transgenic roots, whereas there was no detectable fluorescence in control hairy roots. The enzyme assay showed that the APase activity increased by 2-fold in transgenic hairy roots. The transformed hairy roots displayed an increase in plant soluble P and total P contents, as compared with the control plants, leading to improved biomass production. RT-PCR analysis revealed high expression levels of AtPAP18 in transformed hairy roots. It is noteworthy that these primers amplified no PAP18 transcript in control hairy roots. Taken together, the findings demonstrated that overexpression of the AtPAP18 gene offers an operative tactic to reduce the utilization of inorganic phosphorus (Pi) fertilizer through increased acquisition of soil Pi, especially improving the crop yield on soils low in available P.

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“…The fresh weight increase in transgenic Arabidopsis lines bearing Faseolus vulgaris phosphatase (PvPs2:1) was significantly larger than that in wild type plants at low and high P levels, especially at the latter, accompanying by the upper of total P content and total root length [51]. AtPAP18 (Arabidopsis purple acid phosphatase encoding gene) tobacco plants exhibited significant increase in the acid phosphatase activity leading to an improved biomass production in both P i -deficient and P i -sufficient conditions [52].…”

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“…In both P i -deficient and P i -sufficient conditions 1.41 (total FW) [52] Mitochondrial malate dehydrogenase (MDH) gene from the mycorrhizal fungi Penicillium oxalicum Al-phosphate medium 1.49 (total FW) [47] The same Fe-phosphate medium 1.29 (total FW) [47] The same Ca-phosphate medium 1.28 (total FW) [47] The Table 2 Transgenic plant advantages in biomass production in different stress conditions transcription factor resulted in reduced plant growth compared with the control plants under normal growth conditions [65]. However, the 35S:SlAIM1 plants grow significantly better than the wild-type controls under high salinity, and only marginally lower than the 35S: SlAIM1 plants grown without salt stress.…”

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Biopolym. Cell

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Plant biomass enhancement using transgenesis in model as well as in crop plants both under optimal and stress controlled (greenhouse or growth chamber) and field conditions is observed. It was documented that genetic engineering approaches allow reaching up to twofold increase of biomass in optimal conditions. Both transgenic and initial plants reduce biomass production under stress. It was demonstrated that it can be up to 2-fold increase in productivity of transgenic plant versus untransformed one in stress. Some heterologous gene expression features influencing plant biomass production are discussed.

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

Cited by 15 publications

References 38 publications

The Binding Mode of an ADP Analogue to a Metallohydrolase Mimics the Likely Transition State

The Binding Mode of an ADP Analogue to a Metallohydrolase Mimics the Likely Transition State

Agrobacterium rhizogenes transformed soybeans with AtPAP18 gene show enhanced phosphorus uptake and biomass production

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