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|Título:||Assembly in G1 phase and long-term stability are unique intrinsic features of CENP-A nucleosomes|
|Autor:||Bodor, D. L.|
Valente, L. P.
Mata, J. F.
Black, B. E.
Jansen, L. E. T.
|Editora:||American Society for Cell Biology|
|Citação:||Dani L. Bodor, Luis P. Valente, João F. Mata, Ben E. Black, and Lars E. T. Jansen Assembly in G1 phase and long-term stability are unique intrinsic features of CENP-A nucleosomes Mol. Biol. Cell 2013 24:7 923-932; First Published on January 30, 2013; doi:10.1091/mbc.E13-01-0034|
|Resumo:||Centromeres are the site of kinetochore formation during mitosis. Centromere protein A (CENP-A), the centromere-specific histone H3 variant, is essential for the epigenetic maintenance of centromere position. Previously we showed that newly synthesized CENP-A is targeted to centromeres exclusively during early G1 phase and is subsequently maintained across mitotic divisions. Using SNAP-based fluorescent pulse labeling, we now demonstrate that cell cycle-restricted chromatin assembly at centromeres is unique to CENP-A nucleosomes and does not involve assembly of other H3 variants. Strikingly, stable retention is restricted to the CENP-A/H4 core of the nucleosome, which we find to outlast general chromatin across several cell divisions. We further show that cell cycle timing of CENP-A assembly is independent of centromeric DNA sequences and instead is mediated by the CENP-A targeting domain. Unexpectedly, this domain also induces stable transmission of centromeric nucleosomes, independent of the CENP-A deposition factor HJURP. This demonstrates that intrinsic properties of the CENP-A protein direct its cell cycle-restricted assembly and induces quantitative mitotic transmission of the CENP-A/H4 nucleosome core, ensuring long-term stability and epigenetic maintenance of centromere position.|
|Versão do Editor:||http://www.molbiolcell.org/content/24/7/923.long|
|Aparece nas colecções:||EM - Artigos|
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|Mol. Biol. Cell-2013-Bodor-923-32.pdf||artigo principal||5,8 MB||Adobe PDF||Ver/Abrir|
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