静息状态下人源STIM1分子的表达纯化及结构初探  

Expression, Purification and 2D Classification of Human STIM1 Molecule at Resting State

作　　者：吉仁慈 Ji Renci(College of Life Sciences,Nankai University,Tianjin 300071,China)

机构地区：[1]南开大学生命科学学院,天津300071

出　　处：《南开大学学报（自然科学版）》2020年第2期100-105,共6页Acta Scientiarum Naturalium Universitatis Nankaiensis

摘　　要：Stormal interaction moleculer1 (STIM1)分子作为内质网膜上的钙离子浓度感受器,是CRAC通道的重要组成部分,对于维持细胞内钙离子的稳态发挥重要的作用.本文利用活细胞共聚焦显微成像技术筛选鉴定出静息态STIM1分子突变体,诱导其在真核系统中表达纯化,并利用负染电镜技术,对收集的蛋白单颗粒进行二维(2D)分类,得到静息态人源STIM1分子的近似模型.Stormal interaction moleculer1(STIM1) molecule acts as a calcium ion concentration receptor on the endoplasmic reticulum membrane and is an important component of the CRAC channel. It plays an important role in the maintenance of intracellular calcium ion homeostasis. In this paper, we used live cell confocal microscopy to screen and identify the resting STIM1 mutant, induced their expression and purification in the eukaryotic system. The collected protein single particles were subjected to two-dimensional(2 D) classification to obtain the approximate structure of the resting human STIM1 molecule using the negative staining and electron microscopy technique.

关 键 词：STIM1 CA2+通道 蛋白质表达纯化 冷冻电镜 

分 类 号：Q78[生物学—分子生物学]