How two become one: HJURP dimerization drives CENP-A assembly

Bodor, Dani L; Jansen, Lars E T

http://hdl.handle.net/10400.7/618

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Autores

Bodor, Dani L

Jansen, Lars E T

Resumo(s)

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.

Palavras-chave

Autoantigens Centromere Chromosomal Proteins, Non-Histone DNA-Binding Proteins Humans Nucleosomes Protein Multimerization

URI

http://hdl.handle.net/10400.7/618

Citação

Bodor, D. L., Jansen, L. E. T. (2013). How two become one: HJURP dimerization drives CENP-A assembly. EMBO J., 32(15), 2090–2092.

Editora

Embo Press

DOI

10.1038/emboj.2013.150

Coleções

EM - Artigos

Licença CC

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