沙冬青CBL1蛋白纯化及性质研究  

Purification and Characterization of CBL1 from Ammopiptanthus mongolicus

作　　者：丁志强[1] 尚桂军[1,2] 李娜[2] 聂荣鑫[2] 赵子华[1] 仓怀兴[2] 

机构地区：[1]北京林业大学,北京100083 [2]中国科学院生物物理研究所,北京100101

出　　处：《中国生物工程杂志》2011年第2期23-29,共7页China Biotechnology

摘　　要：CBL是近年来发现的一类钙信号转导蛋白,CBL-CIPK组成的信号通路在植物应答生物和非生物刺激中发挥重要作用。其中CBL1和相应的CIPK在低钾,渗透压,干旱,机械损伤,及冻伤等环境胁迫中发挥重要作用。通过对沙冬青CBL1表面带电氨基酸定点突变,表面赖氨酸甲基化后电荷消除证明了沙冬青CBL1(AmCBL1)在钙离子存在下的非特异性聚集是由于分子间的电荷相互作用引起,三体蛋白很可能是沙冬青CBL1蛋白发挥功能的单位。通过甲基化可以得到聚合状态均一的蛋白,为CBL1晶体生长奠定了基础。CBL is a member of newly identified calcium signal transmitting proteins. CBL-CIPK pathway played an essential role in responding to the biotic and abiotic stimuli in plant. CBL1 and its specified CIPKs are the main executors dealing with various environmental stressed such as low potassium, osmotic, drought, wound, and cold. Site-directed mutation of positive charged amino acid residue and methylation of Lys on the surface demonstrated that the non-specific aggregation of CBL1 from Ammopiptanthus mongolicus （ AmCBLI ） was result from the weak charges interaction between different molecules, and the trimer state may probably be the function unit for the AmCBL1 at the present of Ca^2＋. The homogeneous state of methylated AmCBL1 provided a solid foundation for its crystallization.

关 键 词：沙冬青 CBL1 环境胁迫 甲基化 点突变 纯化 

分 类 号：Q819[生物学—生物工程]