Cargando…
The histone chaperone NASP maintains H3-H4 reservoirs in the early Drosophila embryo
Histones are essential for chromatin packaging, and histone supply must be tightly regulated as excess histones are toxic. To drive the rapid cell cycles of the early embryo, however, excess histones are maternally deposited. Therefore, soluble histones must be buffered by histone chaperones, but th...
Autores principales: | Tirgar, Reyhaneh, Davies, Jonathan P., Plate, Lars, Nordman, Jared T. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10058107/ https://www.ncbi.nlm.nih.gov/pubmed/36930688 http://dx.doi.org/10.1371/journal.pgen.1010682 |
Ejemplares similares
-
Identification of replication fork-associated proteins in Drosophila embryos and cultured cells using iPOND coupled to quantitative mass spectrometry
por: Munden, Alexander, et al.
Publicado: (2022) -
Expanded binding specificity of the human histone chaperone NASP
por: Wang, Huanyu, et al.
Publicado: (2008) -
Distinct histone H3–H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones
por: Liu, Chao-Pei, et al.
Publicado: (2021) -
NASP maintains histone H3–H4 homeostasis through two distinct H3 binding modes
por: Bao, Hongyu, et al.
Publicado: (2022) -
The human histone chaperone sNASP interacts with linker and core histones through distinct mechanisms
por: Wang, Huanyu, et al.
Publicado: (2012)