Assembly in G1 phase and long-term stability are unique intrinsic features of CENP-A nucleosomes
Autor(a) principal: | |
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Data de Publicação: | 2013 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.7/430 |
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. |
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Assembly in G1 phase and long-term stability are unique intrinsic features of CENP-A nucleosomesG1 PhaseNucleosomesCentromeres 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.FCT fellpwships: (SFRH/BD/74284/2010, SFRH/BPD/69115/2010), National Institutes of Health grant: (GM082989), Burroughs Wellcome Fund (Career Award in the Biomedical Sciences), Rita Allen Foundation Scholar Award, Instituto Gulbenkian de Ciência, European Commission FP7 Program, EMBO.American Society for Cell BiologyARCABodor, D. L.Valente, L. P.Mata, J. F.Black, B. E.Jansen, L. E. T.2015-10-22T15:50:15Z2013-04-012013-04-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.7/430engDani 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.E13-01-003410.1091/mbc.E13-01-0034info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2022-11-29T14:34:49Zoai:arca.igc.gulbenkian.pt:10400.7/430Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T16:11:43.300565Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
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 |
spellingShingle |
Assembly in G1 phase and long-term stability are unique intrinsic features of CENP-A nucleosomes Bodor, D. L. G1 Phase Nucleosomes |
title_short |
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_sort |
Assembly in G1 phase and long-term stability are unique intrinsic features of CENP-A nucleosomes |
author |
Bodor, D. L. |
author_facet |
Bodor, D. L. Valente, L. P. Mata, J. F. Black, B. E. Jansen, L. E. T. |
author_role |
author |
author2 |
Valente, L. P. Mata, J. F. Black, B. E. Jansen, L. E. T. |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
ARCA |
dc.contributor.author.fl_str_mv |
Bodor, D. L. Valente, L. P. Mata, J. F. Black, B. E. Jansen, L. E. T. |
dc.subject.por.fl_str_mv |
G1 Phase Nucleosomes |
topic |
G1 Phase Nucleosomes |
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. |
publishDate |
2013 |
dc.date.none.fl_str_mv |
2013-04-01 2013-04-01T00:00:00Z 2015-10-22T15:50:15Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10400.7/430 |
url |
http://hdl.handle.net/10400.7/430 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
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 10.1091/mbc.E13-01-0034 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
American Society for Cell Biology |
publisher.none.fl_str_mv |
American Society for Cell Biology |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
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1799130572902105088 |