Cargando…
Structure of IMPORTIN-4 bound to the H3–H4–ASF1 histone–histone chaperone complex
IMPORTIN-4, the primary nuclear import receptor of core histones H3 and H4, binds the H3–H4 dimer and histone chaperone ASF1 prior to nuclear import. However, how H3–H3–ASF1 is recognized for transport cannot be explained by available crystal structures of IMPORTIN-4–histone tail peptide complexes....
Autores principales: | Bernardes, Natália Elisa, Fung, Ho Yee Joyce, Li, Yang, Chen, Zhe, Chook, Yuh Min |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
National Academy of Sciences
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9499513/ https://www.ncbi.nlm.nih.gov/pubmed/36103578 http://dx.doi.org/10.1073/pnas.2207177119 |
Ejemplares similares
-
Molecular basis of RanGTP-activated nucleosome assembly with Histones H2A-H2B bound to Importin-9
por: Shaffer, Joy M., et al.
Publicado: (2023) -
Importin-9 wraps around the H2A-H2B core to act as nuclear importer and histone chaperone
por: Padavannil, Abhilash, et al.
Publicado: (2019) -
The activity of the histone chaperone yeast Asf1 in the assembly and disassembly of histone H3/H4–DNA complexes
por: Donham, Douglas C., et al.
Publicado: (2011) -
Histone chaperone ASF1 mediates H3.3-H4 deposition in Arabidopsis
por: Zhong, Zhenhui, et al.
Publicado: (2022) -
The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3–H4 tetramers and Asf1–H3–H4 complexes
por: Hammond, Colin M., et al.
Publicado: (2016)