期刊
MOLECULAR BIOLOGY OF THE CELL
卷 24, 期 7, 页码 923-932出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E13-01-0034
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资金
- Fundacao para a Ciencia e a Tecnologia Fellowships [SFRH/BD/74284/2010, SFRH/BPD/69115/2010]
- National Institutes of Health [GM082989]
- Career Award in the Biomedical Sciences from the Burroughs Wellcome Fund
- Rita Allen Foundation Scholar Award
- Fundacao Calouste Gulbenkian and Fundacao para a Ciencia e a Tecnologia [BIA-BCM/100557/2008, BIAPRO/100537/2008]
- European Commission FP7 Program
- EMBO Installation
- Fundação para a Ciência e a Tecnologia [PTDC/BIA-BCM/100557/2008, SFRH/BPD/69115/2010, PTDC/BIA-PRO/100537/2008, SFRH/BD/74284/2010] Funding Source: FCT
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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