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Three-dimensional localization of CENP-A suggests a complex higher order structure of centromeric chromatin
journal contribution
posted on 2023-05-18, 19:27 authored by Owen MarshallOwen Marshall, Marshall, AT, Choo, KHAThe histone H3 variant centromere protein A (CENP-A) is central to centromere formation throughout eukaryotes. A long-standing question in centromere biology has been the organization of CENP-A at the centromere and its implications for the structure of centromeric chromatin. In this study, we describe the three-dimensional localization of CENP-A at the inner kinetochore plate through serial-section transmission electron microscopy of human mitotic chromosomes. At the kinetochores of normal centromeres and at a neocentromere, CENP-A occupies a compact domain at the inner kinetochore plate, stretching across two thirds of the length of the constriction but encompassing only one third of the constriction width and height. Within this domain, evidence of substructure is apparent. Combined with previous chromatin immunoprecipitation results (Saffery, R., H. Sumer, S. Hassan, L.H. Wong, J.M. Craig, K. Todokoro, M. Anderson, A. Stafford, and K.H.A. Choo. 2003. Mol. Cell. 12:509-516; Chueh, A.C., L.H. Wong, N. Wong, and K.H.A. Choo. 2005. Hum. Mol. Genet. 14:85-93), our data suggest that centromeric chromatin is arranged in a coiled 30-nm fiber that is itself coiled or folded to form a higher order structure.
History
Publication title
Journal of Cell BiologyVolume
183Issue
7Pagination
1193-1202ISSN
0021-9525Department/School
Menzies Institute for Medical ResearchPublisher
Rockefeller Univ PressPlace of publication
1114 First Ave, 4Th Fl, New York, USA, Ny, 10021Repository Status
- Restricted