Loading...
Publication
Assembly in G1 phase and long-term stability are unique intrinsic features of CENP-A nucleosomes
| Name: | Description: | Size: | Format: | |
|---|---|---|---|---|
| artigo principal | 5.66 MB | Adobe PDF |
Advisor(s)
Abstract(s)
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.
Description
Keywords
G1 Phase Nucleosomes
Citation
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
Publisher
American Society for Cell Biology