通过FRET受体光漂白，免疫调节药物Bz-423与活细胞中线粒体FoF1-ATP合酶的结合
Binding of the immunomodulatory drug Bz-423 to mitochondrial FoF1-ATP synthase in living cells by FRET acceptor photobleaching
摘要：
Bz-423是一种很有前途的治疗自身免疫性疾病的新药。这种小分子与线粒体酶FoF 1-ATP合酶的亚基OSCP结合并调节其催化活性。我们研究了Bz-423与活细胞中线粒体的结合，以及FoF 1-ATP合酶中的亚基旋转（即该酶的机械化学机制）如何受到Bz-423的影响。因此，通过与荧光蛋白EGFP基因融合到γ亚基的C末端来选择性地标记该酶。利用结构照明显微镜（SIM），可以在超分辨率下对活酵母细胞中线粒体的三维排列进行成像。我们测量了摄取和结合的Cy 5标记的Bz-423衍生物的线粒体FoF 1-ATP合酶在活酵母细胞中使用FRET受体光漂白显微镜。我们的数据证实了Cy 5标记的Bz-423与活酿酒酵母细胞线粒体中酶的F1结构域的顶部结合。
英文摘要：
Bz-423 is a promising new drug for treatment of autoimmune diseases. This small molecule binds to subunit OSCP of the mitochondrial enzyme FoF1-ATP synthase and modulates its catalytic activities. We investigate the binding of Bz-423 to mitochondria in living cells and how subunit rotation in FoF1-ATP synthase, i.e. the mechanochemical mechanism of this enzyme, is affected by Bz-423. Therefore, the enzyme was marked selectively by genetic fusion with the fluorescent protein EGFP to the C terminus of subunit gamma. Imaging the threedimensional arrangement of mitochondria in living yeast cells was possible at superresolution using structured illumination microscopy, SIM. We measured uptake and binding of a Cy5-labeled Bz-423 derivative to mitochondrial FoF1-ATP synthase in living yeast cells using FRET acceptor photobleaching microscopy. Our data confirmed the binding of Cy5-labeled Bz-423 to the top of the F1 domain of the enzyme in mitochondria of living Saccharomyces cerevisiae cells.
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