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

被引：26

作者：

Hellwig, Daniela ^{[1
]}

Munch, Sandra ^{[1
]}

Orthaus, Sandra ^{[1
]}

Hoischen, Christian ^{[1
]}

Hemmerich, Peter ^{[1
]}

Diekmann, Stephan ^{[1
]}

机构：

[1] Leibniz Inst Age Res, Fritz Lipmann Inst, Dept Mol Biol, D-07745 Jena, Germany

来源：

JOURNAL OF BIOPHOTONICS | 2008年 / 1卷 / 03期

关键词：

centromere; kinetochore; mitosis; live-cell imaging; NAC complex; FRAP; FCS; FRET;

D O I：

10.1002/jbio.200810014

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 hole of CENP-T in kinetochore function. (C) 2008 by WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim

引用

页码：245 / 254

页数：10

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