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Three-dimensional localization of CENP-A suggests a complex higher order structure of centromeric chromatin

Citation

Marshall, OJ and Marshall, AT and Choo, KHA, Three-dimensional localization of CENP-A suggests a complex higher order structure of centromeric chromatin, Journal of Cell Biology, 183, (7) pp. 1193-1202. ISSN 0021-9525 (2008) [Refereed Article]

DOI: doi:10.1083/jcb.200804078

Abstract

The 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.

Item Details

Item Type:Refereed Article
Research Division:Biological Sciences
Research Group:Biochemistry and Cell Biology
Research Field:Biochemistry and Cell Biology not elsewhere classified
Objective Division:Expanding Knowledge
Objective Group:Expanding Knowledge
Objective Field:Expanding Knowledge in the Medical and Health Sciences
Author:Marshall, OJ (Dr Owen Marshall)
ID Code:108958
Year Published:2008
Web of Science® Times Cited:39
Deposited By:Menzies Institute for Medical Research
Deposited On:2016-05-12
Last Modified:2016-05-12
Downloads:0

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