OsCML16 以钙/镁依赖和非依赖的方式与水稻中的一个新的 CC-NBS-LRR 蛋白 OsPi304 相互作用。
OsCML16 interacts with a novel CC-NBS-LRR protein OsPi304 in the Ca/Mg dependent and independent manner in rice.
机构信息
MOA Key Laboratory of Crop Ecophysiology and Farming System in the Middle Reaches of the Yangtze River, Huazhong Agricultural University, Wuhan, 430070, China; College of Plant Science and Technology, Huazhong Agricultural University, Wuhan, 430070, China.
Agricultural Technology Extension Center of Wuhan City, Wuhan, Hubei, 430016, China.
出版信息
Biochem Biophys Res Commun. 2018 Sep 26;504(1):346-351. doi: 10.1016/j.bbrc.2018.08.194. Epub 2018 Sep 3.
In plants, many target proteins of calmodulins (CaMs) have been identified in cellular metabolism and responses. However, calmodulin-like proteins (CMLs) and their target proteins have not been discovered in stress responses in rice. In this study, a novel CC-NBS-LRR protein was obtained in screening a cold stress rice seedlings yeast cDNA library with OsCML16 as bait. Furthermore, yeast two-hybrid and BiFC assays demonstrated that the full length, CC region in the N-terminus and LRR in the C-terminus of Pi304 protein could interact with OsCML16. More interestingly, OsCML16 bound to the 1-10 motif rather than 1-14 motif in the Ca or Mg dependent manner in vitro. In addition, transcript levels of OsCML16 and OsPi304 were induced more markedly in Nipponbare than in 9311 under cold stress. Taken together, these data indicates that they are involved in the cold stress signaling and response in rice.
在植物中，许多钙调素（CaMs）的靶蛋白已在细胞代谢和反应中被鉴定出来。然而，在水稻的应激反应中，尚未发现钙调素样蛋白（CMLs）及其靶蛋白。在这项研究中，我们以 OsCML16 为诱饵，从筛选的冷胁迫水稻幼苗酵母 cDNA 文库中获得了一种新型的 CC-NBS-LRR 蛋白。此外，酵母双杂交和 BiFC 实验表明，Pi304 蛋白全长、N 端的 CC 区和 C 端的 LRR 区均可与 OsCML16 相互作用。更有趣的是，OsCML16 在体外以 Ca 或 Mg 依赖性的方式与 1-10 基序而非 1-14 基序结合。此外，在冷胁迫下，Nipponbare 中 OsCML16 和 OsPi304 的转录水平比 9311 中明显升高。综上所述，这些数据表明它们参与了水稻的冷胁迫信号转导和响应。
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