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Interaction between Bax and Bcl-XL proteins confirmed by partial acceptor photobleaching-based FRET imaging
Journal of Innovative Optical Health Sciences ( IF 2.3 ) Pub Date : 2020-02-13 , DOI: 10.1142/s179354582050011x
Fangfang Yang 1 , Mengyan Du 1 , Xiaoping Wang 2 , Tongsheng Chen 1
Affiliation  

Exact interaction mechanism between Bax and Bcl-XL, two key Bcl-2 family proteins, is an interesting and controversial issue. Partial acceptor photobleaching-based quantitative fluorescence resonance energy transfer (FRET) measurement, PbFRET, is a widely used FRET quantification method in living cells. In this report, we implemented pixel-to-pixel PbFRET imaging on a wide-field microscope to map the FRET efficiency ([Formula: see text] images of single living HepG2 cells co-expressing CFP-Bax and YFP-Bcl-XL. The [Formula: see text] value between CFP-Bax and YFP-Bcl-XL was 4.59% in cytosol and 11.31% on mitochondria, conclusively indicating the direct interaction of the two proteins, and the interaction of the two proteins was strong on mitochondria and modest in cytosol.

中文翻译:

基于部分受体光漂白的 FRET 成像证实了 Bax 和 Bcl-XL 蛋白之间的相互作用

Bax 和 Bcl-XL 这两个关键的 Bcl-2 家族蛋白之间的确切相互作用机制是一个有趣且有争议的问题。基于部分受体光漂白的定量荧光共振能量转移 (FRET) 测量 PbFRET 是活细胞中广泛使用的 FRET 定量方法。在本报告中,我们在宽视野显微镜上实现了像素到像素的 PbFRET 成像,以绘制 FRET 效率([公式:见文本] 共表达 CFP-Bax 和 YFP-Bcl-XL 的单个活 HepG2 细胞的图像。 CFP-Bax和YFP-Bcl-XL之间的[公式:见正文]在胞质溶胶中的值为4.59%,在线粒体中为11.31%,最终表明这两种蛋白质的直接相互作用,并且两种蛋白质的相互作用在线粒体上是强的和适度的胞质溶胶。
更新日期:2020-02-13
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