Cargando…
The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution
NAP-1 fold histone chaperones play an important role in escorting histones to and from sites of nucleosome assembly and disassembly. The two NAP-1 fold histone chaperones in budding yeast, Vps75 and Nap1, have previously been crystalized in a characteristic homodimeric conformation. In this study, a...
Autores principales: | Bowman, Andrew, Hammond, Colin M., Stirling, Andrew, Ward, Richard, Shang, Weifeng, El-Mkami, Hassane, Robinson, David A., Svergun, Dmitri I., Norman, David G., Owen-Hughes, Tom |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4027167/ https://www.ncbi.nlm.nih.gov/pubmed/24688059 http://dx.doi.org/10.1093/nar/gku232 |
Ejemplares similares
-
The Histone Chaperones Nap1 and Vps75 Bind Histones H3 and H4 in a Tetrameric Conformation
por: Bowman, Andrew, et al.
Publicado: (2011) -
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) -
Probing the (H3-H4)(2) histone tetramer structure using pulsed EPR spectroscopy combined with site-directed spin labelling
por: Bowman, Andrew, et al.
Publicado: (2010) -
Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75
por: Berndsen, Christopher E, et al.
Publicado: (2008) -
The Cac1 subunit of histone chaperone CAF-1 organizes CAF-1-H3/H4 architecture and tetramerizes histones
por: Liu, Wallace H, et al.
Publicado: (2016)