Dynamic localization of membrane proteins in Bacillus subtilis
Dynamic localization of membrane proteins in Bacillus subtilis
复制标题
DOI：
10.1099/mic.0.27223-0
复制
发表时间：
2004-09-01
期刊：
影响因子：
2.8
通讯作者：
Lewis, PJ
中科院分区：
文献类型：
--
作者：
Johnson, AS;van Horck, S;Lewis, PJ
利用荧光蛋白融合技术对枯草芽孢杆菌膜蛋白的亚细胞定位进行了研究。发现ATP合成酶和琥珀酸脱氢酶定位于膜上的离散区域，而不是像预期的那样均匀地分布在细胞周围。细胞的双重标记表明ATP合成酶和琥珀酸脱氢酶部分共存。进一步使用异位表达的噬菌体蛋白进行分析，得到了与ATP合成酶和琥珀酸脱氢酶相同的定位模式，这意味着膜蛋白仅限于膜内的结构域。ATP合成酶定位的三维重建图像显示，结构域不规则，没有偏向细胞极点或任何其他位置的定位。进一步的分析表明，这种定位是高度动态的，但却是随机的，这意味着完整的膜蛋白可以自由地在细胞膜周围二维扩散。
The subcellular localization of membrane proteins in Bacillus subtilis was examined by using fluorescent protein fusions. ATP synthase and succinate dehydrogenase were found to localize within discrete domains on the membrane rather than being homogeneously distributed around the cell periphery as expected. Dual labelling of cells indicated partial colocalization of ATP synthase and succinate dehydrogenase. Further analysis using an ectopically expressed phage protein gave the same localization patterns as ATP synthase and succinate dehydrogenase, implying that membrane proteins are restricted to domains within the membrane. 3D reconstruction of images of the localization of ATP synthase showed that domains were not regular and there was no bias for localization to cell poles or any other positions. Further analysis revealed that this localization was highly dynamic, but random, implying that integral membrane proteins are free to diffuse two-dimensionally around the cytoplasmic membrane.