Abstract
Phosphorus is an essential macronutrient for plants. The phosphate (Pi) concentration in soil solutions is typically low, and plants always suffer from low-Pi stress. During Pi starvation, a number of adaptive mechanisms in plants have evolved to increase Pi uptake, whereas the mechanisms are not very clear. Here, we report that an ubiquitin E3 ligase, PRU2, modulates Pi acquisition in Arabidopsis response to the low-Pi stress. The mutant pru2 showed arsenate-resistant phenotypes and reduced Pi content and Pi uptake rate. The complementation with PRU2 restored these to wild-type plants. PRU2 functioned as an ubiquitin E3 ligase, and the protein accumulation of PRU2 was elevated during Pi starvation. PRU2 interacted with a kinase CK2α1 and a ribosomal protein RPL10 and degraded CK2α1 and RPL10 under low-Pi stress. The in vitro phosphorylation assay showed that CK2α1 phosphorylated PHT1;1 at Ser-514, and prior reports demonstrated that the phosphorylation of PHT1;1 Ser-514 resulted in PHT1;1 retention in the endoplasmic reticulum. Then, the degradation of CK2α1 by PRU2 under low-Pi stress facilitated PHT1;1 to move to the plasma membrane to increase Arabidopsis Pi uptake. Taken together, this study demonstrated that the ubiquitin E3 ligase-PRU2-was an important positive regulator in modulating Pi acquisition in Arabidopsis response to low-Pi stress.