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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...
Tallennettuna:
| Julkaisussa: | Nucleic Acids Res |
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| Päätekijät: | , , , , , , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Oxford University Press
2016
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5291247/ https://ncbi.nlm.nih.gov/pubmed/27036862 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/nar/gkw209 |
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