Please use this identifier to cite or link to this item: http://hdl.handle.net/10400.7/618
Title: How two become one: HJURP dimerization drives CENP-A assembly
Author: Bodor, Dani L
Jansen, Lars E T
Keywords: Autoantigens
Centromere
Chromosomal Proteins, Non-Histone
DNA-Binding Proteins
Humans
Nucleosomes
Protein Multimerization
Issue Date: 21-Jun-2013
Publisher: Embo Press
Citation: Bodor, D. L., Jansen, L. E. T. (2013). How two become one: HJURP dimerization drives CENP-A assembly. EMBO J., 32(15), 2090–2092.
Abstract: CENP‐A containing nucleosomes epigenetically specify centromere position on chromosomes. Deposition of CENP‐A into chromatin is mediated by HJURP, a specific CENP‐A chaperone. Paradoxically, HJURP binding sterically prevents dimerization of CENP‐A, which is critical to form functional centromeric nucleosomes. A recent publication in The EMBO Journal (Zasadzińska et al, 2013) demonstrates that HJURP itself dimerizes through a C‐terminal repeat region, which is essential for centromeric assembly of nascent CENP‐A.
Peer review: yes
URI: http://hdl.handle.net/10400.7/618
DOI: 10.1038/emboj.2013.150
Publisher Version: http://emboj.embopress.org/content/32/15/2090
Appears in Collections:EM - Artigos

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