Cargando…
Replication-independent nucleosome exchange is enhanced by local and specific acetylation of histone H4
We used a novel single-cell strategy to examine the fate of histones during G(2)-phase. Consistent with previous results, we find that in G(2)-phase, the majority of nuclear histones are assembled into chromatin, whereas a small fraction comprises an unassembled pool. Small increases in the amount o...
Autores principales: | Elliott, Giles O., Murphy, Kevin J., Hayes, Jeffrey J., Thiriet, Christophe |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3575802/ https://www.ncbi.nlm.nih.gov/pubmed/23303778 http://dx.doi.org/10.1093/nar/gks1451 |
Ejemplares similares
-
Contributions of histone tail clipping and acetylation in nucleosome transcription by RNA polymerase II
por: Oishi, Takumi, et al.
Publicado: (2023) -
Histone protein surface accessibility dictates direction of RSC-dependent nucleosome mobilization
por: Bhat, Javeed Ahmad, et al.
Publicado: (2022) -
Genome-wide H4 K16 acetylation by SAS-I is deposited independently of transcription and histone exchange
por: Heise, Franziska, et al.
Publicado: (2012) -
DNA and nucleosomes direct distinct folding of a linker histone H1 C-terminal domain
por: Fang, He, et al.
Publicado: (2012) -
Super-resolution microscopy reveals how histone tail acetylation affects DNA compaction within nucleosomes in vivo
por: Otterstrom, Jason, et al.
Publicado: (2019)