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J Biophotonics. 2008 Aug;1(3):245-54. doi: 10.1002/jbio.200810014.

Live-cell imaging reveals sustained centromere binding of CENP-T via CENP-A and CENP-B.

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  • 1Leibniz-Institute for Age Research - Fritz Lipmann Institute, Dept. of Molecular Biology, Beutenbergstr. 11, D-07745 Jena, Germany.


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.

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