Chromosomes. CENP-C reshapes and stabilizes CENP-A nucleosomes at the centromere
Inheritance of each chromosome depends upon its centromere. A histone H3 variant, centromere protein A (CENP-A), is essential for epigenetically marking centromere location. We find that CENP-A is quantitatively retained at the centromere upon which it is initially assembled. CENP-C binds to CENP-A...
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| Outros Autores: | , , , , , , , , , , |
| Formato: | article |
| Idioma: | eng |
| Publicado em: |
2016
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| Assuntos: | |
| Texto completo: | http://hdl.handle.net/10400.7/627 |
| País: | Portugal |
| Oai: | oai:arca.igc.gulbenkian.pt:10400.7/627 |
| Resumo: | Inheritance of each chromosome depends upon its centromere. A histone H3 variant, centromere protein A (CENP-A), is essential for epigenetically marking centromere location. We find that CENP-A is quantitatively retained at the centromere upon which it is initially assembled. CENP-C binds to CENP-A nucleosomes and is a prime candidate to stabilize centromeric chromatin. Using purified components, we find that CENP-C reshapes the octameric histone core of CENP-A nucleosomes, rigidifies both surface and internal nucleosome structure, and modulates terminal DNA to match the loose wrap that is found on native CENP-A nucleosomes at functional human centromeres. Thus, CENP-C affects nucleosome shape and dynamics in a manner analogous to allosteric regulation of enzymes. CENP-C depletion leads to rapid removal of CENP-A from centromeres, indicating their collaboration in maintaining centromere identity. |
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