Biotechnology Research Institute; Chinese Academy of Agricultural Sciences; Beijing, PR China.
School of Life Sciences; Chongqing University; Chongqing, PR China.
Plant Signal Behav. 2013 Nov;8(11):e26115. doi: 10.4161/psb.26115. Epub 2013 Aug 29.
FKBP12 encodes a prolyl isomerase and highly conserved in eukaryotic species. In yeasts and animals, FKBP12 can interact with rapamycin and FK506 to form rapamycin-FKBP12 and FK506-FKBP12 complex, respectively. In higher plants, FKBP12 protein lost its function to bind rapamycin and FK506. Early studies showed that yeast and human FKBP12 protein can restore the rapamycin sensitivity in Arabidopsis, but the used concentration is 100-1000 folds higher than that in yeast and animals. High concentration of drugs would increase the cost and cause the potential secondary effects on plant growth and development. Here we further discovered that BP12 plants generated in our previous study are hypersensitive to rapamycin at the concentration as low as that is effective in yeast and animals. It is surprising to observe that WT and BP12 plants are not sensitive to FK506 in normal growth condition. These findings advance the current understanding of rapamycin-TOR signaling in plants.
FKBP12 编码一种脯氨酰异构酶,在真核生物中高度保守。在酵母和动物中,FKBP12 可以分别与雷帕霉素和 FK506 相互作用,形成雷帕霉素-FKBP12 和 FK506-FKBP12 复合物。在高等植物中,FKBP12 蛋白失去了与雷帕霉素和 FK506 结合的功能。早期研究表明,酵母和人类 FKBP12 蛋白可以恢复拟南芥中雷帕霉素的敏感性,但所用浓度比酵母和动物高 100-1000 倍。高浓度的药物会增加成本,并对植物的生长和发育产生潜在的副作用。在这里,我们进一步发现,在我们之前的研究中生成的 BP12 植物对雷帕霉素的敏感性在低浓度下就像在酵母和动物中那样有效。令人惊讶的是,在正常生长条件下,WT 和 BP12 植物对 FK506 不敏感。这些发现推进了我们对植物中雷帕霉素-TOR 信号的理解。