How two become one: HJURP dimerization drives CENP-A assembly
| Data(s) |
24/05/2016
24/05/2016
21/06/2013
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|---|---|
| Resumo |
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. FCT fellowship: (SFRH/BD/74284/2010); FCT grants: (BIA-BCM/100557/2008, BIAPRO/100537/2008); EMBO Installation Grant. |
| Identificador |
Bodor, D. L., Jansen, L. E. T. (2013). How two become one: HJURP dimerization drives CENP-A assembly. EMBO J., 32(15), 2090–2092. http://hdl.handle.net/10400.7/618 10.1038/emboj.2013.150 |
| Idioma(s) |
eng |
| Publicador |
Embo Press |
| Relação |
http://emboj.embopress.org/content/32/15/2090 |
| Direitos |
openAccess http://creativecommons.org/licenses/by/4.0/ |
| Palavras-Chave | #Autoantigens #Centromere #Chromosomal Proteins, Non-Histone #DNA-Binding Proteins #Humans #Nucleosomes #Protein Multimerization |
| Tipo |
article |
