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OsHAD1, a haloacid dehalogenase-like APase enhances phosphate accumulation

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Title OsHAD1, a haloacid dehalogenase-like APase enhances phosphate accumulation
 
Creator Pandey, Bipin Kumar
Mehra, Poonam
Verma, Lokesh
Bhadouria, Jyoti
Giri, Jitender
 
Subject OsHAD1
phosphate
haloacid
 
Description Accepted date: June 17, 2017
Phosphorus (P) deficiency limits plant growth and crop yield. Since, plants can absorb only inorganic form of P (Pi), a large portion of soil P (organic and inorganic P complexes) remains largely unused. Here, we identified and characterized a PHR2 regulated; novel low Pi responsive haloacid dehalogenase (HAD)-like hydrolase, OsHAD1. While, OsHAD1 is a functional HAD protein having both acid phosphatase and phytase activity; it showed little homology with other known low Pi responsive HAD superfamily members. Recombinant OsHAD1 is highly active at acidic pH and dephosphorylates broad range of organic and inorganic P containing substrates including protein phosphates and Na-phytate. Exogenous application of recombinant OsHAD1 protein in growth media supplemented with phytate, led to marked increase in growth and total P content of Pi deficient WT rice seedlings. Further, overexpression of OsHAD1 in rice resulted in enhanced phosphatase activity, biomass, total and soluble P content in Pi deficient transgenic seedlings treated with phytate as restricted Pi source. Gene expression and metabolite profiling revealed enhanced Pi starvation responses such as upregulation of multiple genes involved in Pi uptake and solubilization, accumulation of organic acids, enhanced secretory phosphatase activity and depletion of ATP in overexpression lines as compared to WT. To elucidate the underlying regulatory mechanisms of OsHAD1, we performed in-vitro pull down assays which revealed association of OsHAD1 with protein kinases. We conclude that besides dephosphorylation of cellular organic-P, OsHAD1 in coordination with kinases may regulate phosphorylation status of downstream targets to accomplish Pi homeostasis under limited Pi supply.
Our work is supported by the research grant of DBT (Grant No.
32 BT/PR3299/AGR/2/813/2011), Government of India and NIPGR core grants.
 
Date 2017-06-28T10:14:37Z
2017-06-28T10:14:37Z
2017
 
Type Article
 
Identifier Plant Physiology, 174(4): 2316-2332
1532-2548
http://59.163.192.83:8080/jspui/handle/123456789/764
http://www.plantphysiol.org/content/early/2017/06/21/pp.17.00571.long
https://doi.org/10.1104/pp.17.00571
 
Language en_US
 
Publisher American Society of Plant Biologists