FCCC LOGO Faculty Publications
Sugata N , Li SL , Earnshaw WC , Yen TJ , Yoda K , Masumoto H , Munekata E , Warburton PE , Todokoro K
Human CENP-H multimers colocalize with CENP-A and CENP-C at active centromere-kinetochore complexes
Human Molecular Genetics. 2000 Nov 22;9(19) :2919-2926
PMID: ISI:000165620300015   
Back to previous list
Abstract
Centromere and kinetochore proteins have a pivotal role in centromere structure, kinetochore formation;Ind 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.
Notes
Times Cited: 9 English Article 379BD HUM MOL GENET