Hellwig Daniela, Münch Sandra, Orthaus Sandra, Hoischen Christian, Hemmerich Peter, Diekmann Stephan
Leibniz-Institute for Age Research - Fritz Lipmann Institute, Dept. of Molecular Biology, Beutenbergstr. 11, D-07745 Jena, Germany.
J Biophotonics. 2008 Aug;1(3):245-54. doi: 10.1002/jbio.200810014.
At the centromere, a network of proteins, the kinetochore, assembles in order to grant correct chromatin segregation. In this study the dynamics and molecular interactions of the inner kinetochore protein CENP-T were analyzed employing a variety of fluorescence microscopy techniques in living human cells. Acceptor-bleaching FRET indicates that CENP-T directly associates with CENP-A and CENP-B. CENP-T exchange into centromeres is restricted to the S-phase of the cell cycle as revealed by FRAP, suggesting a coreplicational loading mechanism, as we have recently also demonstrated for CENP-I. These properties make CENP-T one of the basic inner kinetochore proteins with most further proteins binding downstream, suggesting a fundamental role of CENP-T in kinetochore function.
在着丝粒处，一个由蛋白质组成的网络，即动粒，会组装起来以确保染色质的正确分离。在这项研究中，利用多种荧光显微镜技术在活的人类细胞中分析了动粒内部蛋白CENP-T的动力学和分子相互作用。受体漂白荧光共振能量转移表明CENP-T直接与CENP-A和CENP-B相关联。荧光漂白恢复实验显示，CENP-T向着丝粒的交换仅限于细胞周期的S期，这表明存在一种共复制加载机制，正如我们最近对CENP-I所证明的那样。这些特性使CENP-T成为动粒内部的基本蛋白之一，大多数其他蛋白在其下游与之结合，这表明CENP-T在动粒功能中具有重要作用。
