The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3–H4 tetramers and Asf1–H3–H4 complexes

Vps75 is a histone chaperone that has been historically characterized as homodimer by X-ray crystallography. In this study, we present a crystal structure containing two related tetrameric forms of Vps75 within the crystal lattice. We show Vps75 associates with histones in multiple oligomers. In the...

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Detalles Bibliográficos
Autores principales: Hammond, Colin M., Sundaramoorthy, Ramasubramanian, Larance, Mark, Lamond, Angus, Stevens, Michael A., El-Mkami, Hassane, Norman, David G., Owen-Hughes, Tom
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2016
Materias:
Gene regulation, Chromatin and Epigenetics
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5291247/
https://www.ncbi.nlm.nih.gov/pubmed/27036862
http://dx.doi.org/10.1093/nar/gkw209

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5291247/
https://www.ncbi.nlm.nih.gov/pubmed/27036862
http://dx.doi.org/10.1093/nar/gkw209

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