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Human Molecular Genetics, 2000, Vol. 9, No. 19 2919-2926
© 2000 Oxford University Press

Human CENP-H multimers colocalize with CENP-A and CENP-C at active centromere–kinetochore complexes

Naoko Sugata1,2, Shulan Li3, William C. Earnshaw4, Tim J. Yen5, Kinya Yoda6, Hiroshi Masumoto7, Eisuke Munekata2, Peter E. Warburton3 and Kazuo Todokoro1,+

1Tsukuba Life Science Center, The Institute of Physical and Chemical Research (RIKEN), 3-1 Koyadai, Tsukuba, Ibaraki 305-0074, Japan, 2Institute of Applied Biochemistry, Tsukuba University, Tennoudai, Tsukuba, Ibaraki 305-8572, Japan, 3Department of Human Genetics, Mount Sinai School of Medicine, 1425 Madison Avenue, New York, NY 10029, USA, 4Wellcome Trust Centre for Cell Biology, ICMB, University of Edinburgh, King’s Buildings, Mayfield Road, Edinburgh EH9 3JR, UK, 5Fox Chase Cancer Center, 7701 Burholme Avenue, Philadelphia, PA 19111, USA, 6Bioscience Center, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-01, Japan and 7Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan

Centromere and kinetochore proteins have a pivotal role in centromere structure, kinetochore formation and sister chromatid separation. However, the molecular architecture and the precise dynamic function of the centromere–kinetochore complex during mitosis remain poorly understood. Here we report the isolation and characterization of human CENP-H. Confocal microscopic analyses of HeLa cells with anti-human CENP-H-specific antibody demonstrated that CENP-H colocalizes with inner kinetochore plate proteins CENP-A and CENP-C in both interphase and metaphase. CENP-H was present outside centromeric heterochromatin, where CENP-B is localized, and inside the kinetochore corona, where CENP-E is localized during prometaphase. Furthermore, CENP-H was detected at neocentromeres, but not at inactive centromeres in stable dicentric chromosomes. In vitro binding assays of human CENP-H with centromere–kinetochore proteins suggest that the CENP-H binds to itself and MCAK, but not to CENP-A, CENP-B or CENP-C. CENP-H multimers were observed in cells in which both FLAG-tagged CENP-H and hemagglutinin-tagged CENP-H were expressed. These results suggest that CENP-H multimers localize constitutively to the inner kinetochore plate and play an important fundamental role in organization and function of the active human centromere–kinetochore complex.

+ To whom correspondence should be addressed. Tel: +81 298 36 9075; Fax: +81 298 36 9090; Email: todokoro@rtc.riken.go.jp


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