Wu Jian-Qiu, Pollard Thomas D
Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520-8103, USA.
Science. 2005 Oct 14;310(5746):310-4. doi: 10.1126/science.1113230.
We used fluorescence microscopy to measure global and local concentrations of 28 cytoskeletal and signaling proteins fused to yellow fluorescent protein (YFP) in the fission yeast Schizosaccharomyces pombe. Native promoters controlled the expression of these functional YFP fusion proteins. Fluorescence measured by microscopy or flow cytometry was directly proportional to protein concentration measured by quantitative immunoblotting. Global cytoplasmic concentrations ranged from 0.04 (formin Cdc12p) to 63 micromolar (actin). Proteins concentrated up to 100 times in contractile rings and 7500 times in spindle pole bodies at certain times in the cell cycle. This approach can be used to measure the global and local concentrations of any fusion protein.
我们利用荧光显微镜测量了粟酒裂殖酵母中28种与黄色荧光蛋白(YFP)融合的细胞骨架和信号蛋白的整体及局部浓度。天然启动子控制这些功能性YFP融合蛋白的表达。通过显微镜或流式细胞术测量的荧光与通过定量免疫印迹法测量的蛋白质浓度直接成正比。整体细胞质浓度范围从0.04微摩尔(formin Cdc12p)到63微摩尔(肌动蛋白)。在细胞周期的特定时间,蛋白质在收缩环中浓缩高达100倍,在纺锤极体中浓缩高达7500倍。这种方法可用于测量任何融合蛋白的整体及局部浓度。