Structure analysis of S. cerevisiae Rap1-telomeric DNA complex by electron microscopy

端粒是一种特殊的核蛋白复合体，它覆盖在真核线性染色体的末端，稳定它们并保护它们的完整性。在芽殖酵母中，主要的端粒结合蛋白Rap1控制端粒的长度。我们制备了RAP1和GFP融合RAP1，并用电子显微镜分析了它们的结构。电子断层扫描和高分辨率荧光显微镜显示了由Rap1制成的独特细丝的三维结构。

Telomeres are specialized nucleoprotein complexes that cap the ends of eukaryotic linear chromosomes, stabilizing them and protecting their integrity. In budding yeast major telomere binding protein Rap1 controls telomere length. We prepared Rap1 and GFP fusion Rap1, and analyzed their structures by electron microscopy. Electron tomography and high resolution fluorescence microscopy revealed three-dimensional structures of unique filaments made of Rap1.