4.7 Article

Maize ZmPT7 regulates Pi uptake and redistribution which is modulated by phosphorylation

期刊

PLANT BIOTECHNOLOGY JOURNAL
卷 18, 期 12, 页码 2406-2419

出版社

WILEY
DOI: 10.1111/pbi.13414

关键词

phosphate acquisition; phosphate redistribution; ZmPT7; phosphorylation modification; maize; Arabidopsis

资金

  1. National Key Research and Development Program of China [2016YFD0100707]
  2. Ministry of Agriculture of China for transgenic research [2016ZX08009002]
  3. National Natural Science Foundation of China [31670245, 31970273]
  4. Chinese Universities Scientific Fund [2019TC122, 2019TC228]
  5. Beijing Outstanding University Discipline Program

向作者/读者索取更多资源

Phosphorus, an essential mineral macronutrient, is a major constituent of fertilizers for maize (Zea mays L.) production. However, the molecular mechanisms of phosphate (Pi) acquisition in maize plants and its redistribution remain unclear. This study presents the functional characterization of ZmPT7 in Pi uptake and redistribution in maize. The ZmPT7 was expressed in roots and leaves, and induced during Pi starvation. The ZmPT7 complemented the Pi-uptake deficiency of yeast mutant pho Delta null and Arabidopsis mutant pht1;1 Delta 4 Delta, indicating that ZmPT7 functioned as a Pi transporter. We generated zmpt7 mutants by CRISPR/Cas9 and ZmPT7-overexpressing lines. The zmpt7 mutants showed reduced, whereas the ZmPT7-overexpressing lines displayed increased Pi-uptake capacity and Pi redistribution from old to young leaves, demonstrating that ZmPT7 played central roles in Pi acquisition and Pi redistribution from old to young leaves. The ZmCK2 kinases phosphorylated ZmPT7 at Ser-521 in old maize leaves, which enhanced transport activity of ZmPT7. The Ser-520 of Arabidopsis AtPHT1;1, a conserved residue of ZmPT7 Ser-521, was also phosphorylated by AtCK2 kinase, and the mutation of Ser-520 to Glu (phosphorylation mimic) yielded enhanced transport activity of AtPHT1;1. Taken together, these results indicate that ZmPT7 plays important roles in Pi acquisition and redistribution, and its transport activity is modulated by phosphorylation.

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