期刊
NATURE COMMUNICATIONS
卷 11, 期 1, 页码 -出版社
NATURE PORTFOLIO
DOI: 10.1038/s41467-020-16695-7
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资金
- Austrian Science Fund (FWF) [FWF W011-B18 DK, P31377-B30]
- Wellcome Senior Research Fellowship
- Instituto Gulbenkian de Ciencia [ERC-2013-CoG-615638]
- ERCconsolidator grant [ERC-2013-CoG-615638]
- European Research Council StartingConsolidator Grant [311674-BioSynCEN]
- Wellcome Trust [103897/Z/14/Z, 092076, 203149]
- Multi-User Equipment grant [101527/Z/13/Z]
- Austrian Science Fund (FWF) [P31377] Funding Source: Austrian Science Fund (FWF)
- Wellcome Trust [103897/Z/14/Z, 101527/Z/13/Z] Funding Source: Wellcome Trust
Replication and transcription of genomic DNA requires partial disassembly of nucleosomes to allow progression of polymerases. This presents both an opportunity to remodel the underlying chromatin and a danger of losing epigenetic information. Centromeric transcription is required for stable incorporation of the centromere-specific histone dCENP-A in M/G1 phase, which depends on the eviction of previously deposited H3/H3.3-placeholder nucleosomes. Here we demonstrate that the histone chaperone and transcription elongation factor Spt6 spatially and temporarily coincides with centromeric transcription and prevents the loss of old CENP-A nucleosomes in both Drosophila and human cells. Spt6 binds directly to dCENP-A and dCENP-A mutants carrying phosphomimetic residues alleviate this association. Retention of phosphomimetic dCENP-A mutants is reduced relative to wildtype, while non-phosphorylatable dCENP-A retention is increased and accumulates at the centromere. We conclude that Spt6 acts as a conserved CENP-A maintenance factor that ensures long-term stability of epigenetic centromere identity during transcription-mediated chromatin remodeling.
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