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Plant Cell Advance Online Publication
Published on December 30, 2005; 10.1105/tpc.105.038943

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Received October 20, 2005
Returned for revision November 24, 2005
Accepted December 12, 2005

Regulation of Phosphate Homeostasis by MicroRNA in Arabidopsis

Tzyy-Jen Chiou 1*, Kyaw Aung 2, Shu-I Lin 3, Chia-Chune Wu 1, Su-Fen Chiang 1, and Chun-lin Su 1

1 Institute of BioAgricultural Sciences, Academia Sinica, Taipei 115, Taiwan, Republic of China
2 Institute of BioAgricultural Sciences, Academia Sinica, Taipei 115, Taiwan, Republic of China; Molecular and Biological Agricultural Sciences Program, Taiwan International Graduate Program, Academia Sinica, Taipei 115, Taiwan, Republic of China
3 Institute of BioAgricultural Sciences, Academia Sinica, Taipei 115, Taiwan, Republic of China; Graduate Institute of Life Sciences, National Defense Medical Center, Taipei 114, Taiwan, Republic of China

* To whom correspondence should be addressed. E-mail: tjchiou{at}gate.sinica.edu.tw.

In this study, we reveal a mechanism by which plants regulate inorganic phosphate (Pi) homeostasis to adapt to environmental changes in Pi availability. This mechanism involves the suppression of a ubiquitin-conjugating E2 enzyme by a specific microRNA, miR399. Upon Pi starvation, the miR399 is upregulated and its target gene, a ubiquitin-conjugating E2 enzyme, is downregulated in Arabidopsis thaliana. Accumulation of the E2 transcript is suppressed in transgenic Arabidopsis overexpressing miR399. Transgenic plants accumulated five to six times the normal Pi level in shoots and displayed Pi toxicity symptoms that were phenocopied by a loss-of-function E2 mutant. Pi toxicity was caused by increased Pi uptake and by translocation of Pi from roots to shoots and retention of Pi in the shoots. Moreover, unlike wild-type plants, in which Pi in old leaves was readily retranslocated to other developing young tissues, remobilization of Pi in miR399-overexpressing plants was impaired. These results provide evidence that miRNA controls Pi homeostasis by regulating the expression of a component of the proteolysis machinery in plants.




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