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

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 nu...

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Detalhes bibliográficos
Autor principal: Bodor, Dani L (author)
Outros Autores: Jansen, Lars E T (author)
Formato: article
Idioma:eng
Publicado em: 2016
Assuntos:
Autoantigens
Centromere
Chromosomal Proteins, Non-Histone
DNA-Binding Proteins
Humans
Nucleosomes
Protein Multimerization
Texto completo:http://hdl.handle.net/10400.7/618
País:Portugal
Oai:oai:arca.igc.gulbenkian.pt:10400.7/618
Descrição
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.

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