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Vacuolar Proton Pyrophosphatase Is Required for High Magnesium Tolerance in Arabidopsis

1
Nanjing University-Nanjing Forestry University Joint Institute for Plant Molecular Biology, College of Life Sciences, Nanjing University, Nanjing 210093, China
2
Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720, USA
3
Department of Biology, Tokyo Gakugei University, Koganei, Tokyo 184-8501, Japan
4
Nanjing University-Nanjing Forestry University Joint Institute for Plant Molecular Biology, Key Laboratory of Forest Genetics and Biotechnology, Nanjing Forestry University, Nanjing 210037, China
5
College of Agriculture, Ludong University, Yantai 264025, China
*
Authors to whom correspondence should be addressed.
Int. J. Mol. Sci. 2018, 19(11), 3617; https://doi.org/10.3390/ijms19113617
Received: 24 October 2018 / Revised: 11 November 2018 / Accepted: 11 November 2018 / Published: 16 November 2018
(This article belongs to the Section Molecular Plant Sciences)
Magnesium (Mg2+) is an essential nutrient in all organisms. However, high levels of Mg2+ in the environment are toxic to plants. In this study, we identified the vacuolar-type H+-pyrophosphatase, AVP1, as a critical enzyme for optimal plant growth under high-Mg conditions. The Arabidopsis avp1 mutants displayed severe growth retardation, as compared to the wild-type plants upon excessive Mg2+. Unexpectedly, the avp1 mutant plants retained similar Mg content to wild-type plants under either normal or high Mg conditions, suggesting that AVP1 may not directly contribute to Mg2+ homeostasis in plant cells. Further analyses confirmed that the avp1 mutant plants contained a higher pyrophosphate (PPi) content than wild type, coupled with impaired vacuolar H+-pyrophosphatase activity. Interestingly, expression of the Saccharomyces cerevisiae cytosolic inorganic pyrophosphatase1 gene IPP1, which facilitates PPi hydrolysis but not proton translocation into vacuole, rescued the growth defects of avp1 mutants under high-Mg conditions. These results provide evidence that high-Mg sensitivity in avp1 mutants possibly resulted from elevated level of cytosolic PPi. Moreover, genetic analysis indicated that mutation of AVP1 was additive to the defects in mgt6 and cbl2 cbl3 mutants that are previously known to be impaired in Mg2+ homeostasis. Taken together, our results suggest AVP1 is required for cellular PPi homeostasis that in turn contributes to high-Mg tolerance in plant cells. View Full-Text
Keywords: vacuolar H+-pyrophosphatase; AtAVP1; cellular PPi homeostasis; high-Mg tolerance vacuolar H+-pyrophosphatase; AtAVP1; cellular PPi homeostasis; high-Mg tolerance
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Yang, Y.; Tang, R.-J.; Mu, B.; Ferjani, A.; Shi, J.; Zhang, H.; Zhao, F.; Lan, W.-Z.; Luan, S. Vacuolar Proton Pyrophosphatase Is Required for High Magnesium Tolerance in Arabidopsis. Int. J. Mol. Sci. 2018, 19, 3617.

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