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Live‐cell imaging reveals sustained centromere binding of CENP‐T via CENP‐A and CENP‐B
Author(s) -
Hellwig D.,
Münch S.,
Orthaus S.,
Hoischen C.,
Hemmerich P.,
Diekmann S.
Publication year - 2008
Publication title -
journal of biophotonics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.877
H-Index - 66
eISSN - 1864-0648
pISSN - 1864-063X
DOI - 10.1002/jbio.200810014
Subject(s) - centromere , kinetochore , chromatin , microbiology and biotechnology , förster resonance energy transfer , biophysics , aurora b kinase , function (biology) , chemistry , biology , fluorescence , chromosome , genetics , physics , dna , gene , optics
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. (© 2008 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)