Molecular mechanisms underpinning phosphorus‐use efficiency in rice |
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Authors: | D.M.S.B. Dissanayaka William C. Plaxton Hans Lambers Meike Siebers Buddhi Marambe Jun Wasaki |
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Affiliation: | 1. Graduate School of Biosphere Science, Hiroshima University, Hiroshima, Japan;2. Department of Crop Science, Faculty of Agriculture, University of Peradeniya, Peradeniya, Sri Lanka;3. Department of Biology and Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, Canada;4. School of Biological Sciences and Institute of Agriculture, The University of Western Australia, Crawley (Perth), Western Australia, Australia;5. Max‐Planck‐Institute for Plant Breeding Research, Cologne, Germany |
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Abstract: | Orthophosphate (H2PO4?, Pi) is an essential macronutrient integral to energy metabolism as well as a component of membrane lipids, nucleic acids, including ribosomal RNA, and therefore essential for protein synthesis. The Pi concentration in the solution of most soils worldwide is usually far too low for maximum growth of crops, including rice. This has prompted the massive use of inefficient, polluting, and nonrenewable phosphorus (P) fertilizers in agriculture. We urgently need alternative and more sustainable approaches to decrease agriculture's dependence on Pi fertilizers. These include manipulating crops by (a) enhancing the ability of their roots to acquire limiting Pi from the soil (i.e. increased P‐acquisition efficiency) and/or (b) increasing the total biomass/yield produced per molecule of Pi acquired from the soil (i.e. increased P‐use efficiency). Improved P‐use efficiency may be achieved by producing high‐yielding plants with lower P concentrations or by improving the remobilization of acquired P within the plant so as to maximize growth and biomass allocation to developing organs. Membrane lipid remodelling coupled with hydrolysis of RNA and smaller P‐esters in senescing organs fuels P remobilization in rice, the world's most important cereal crop. |
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Keywords: | membrane lipid remodelling phosphorus remobilization purple acid phosphatase (PAP) RNase |
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