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Assembly in G1 phase and long-term stability are unique intrinsic features of CENP-A nucleosomes
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 d...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3608502/ https://www.ncbi.nlm.nih.gov/pubmed/23363600 http://dx.doi.org/10.1091/mbc.E13-01-0034 |
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author | Bodor, Dani L. Valente, Luis P. Mata, João F. Black, Ben E. Jansen, Lars E. T. |
author_facet | Bodor, Dani L. Valente, Luis P. Mata, João F. Black, Ben E. Jansen, Lars E. T. |
author_sort | Bodor, Dani L. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-3608502 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-36085022013-06-16 Assembly in G1 phase and long-term stability are unique intrinsic features of CENP-A nucleosomes Bodor, Dani L. Valente, Luis P. Mata, João F. Black, Ben E. Jansen, Lars E. T. Mol Biol Cell Articles 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. The American Society for Cell Biology 2013-04-01 /pmc/articles/PMC3608502/ /pubmed/23363600 http://dx.doi.org/10.1091/mbc.E13-01-0034 Text en © 2013 Bodor et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell BD; are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Bodor, Dani L. Valente, Luis P. Mata, João F. Black, Ben E. Jansen, Lars E. T. Assembly in G1 phase and long-term stability are unique intrinsic features of CENP-A nucleosomes |
title | Assembly in G1 phase and long-term stability are unique intrinsic features of CENP-A nucleosomes |
title_full | Assembly in G1 phase and long-term stability are unique intrinsic features of CENP-A nucleosomes |
title_fullStr | Assembly in G1 phase and long-term stability are unique intrinsic features of CENP-A nucleosomes |
title_full_unstemmed | Assembly in G1 phase and long-term stability are unique intrinsic features of CENP-A nucleosomes |
title_short | Assembly in G1 phase and long-term stability are unique intrinsic features of CENP-A nucleosomes |
title_sort | assembly in g1 phase and long-term stability are unique intrinsic features of cenp-a nucleosomes |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3608502/ https://www.ncbi.nlm.nih.gov/pubmed/23363600 http://dx.doi.org/10.1091/mbc.E13-01-0034 |
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