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The conformational flexibility of the C-terminus of histone H4 promotes histone octamer and nucleosome stability and yeast viability
BACKGROUND: The protein anti-silencing function 1 (Asf1) chaperones histones H3/H4 for assembly into nucleosomes every cell cycle as well as during DNA transcription and repair. Asf1 interacts directly with H4 through the C-terminal tail of H4, which itself interacts with the docking domain of H2A i...
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| Autori principali: | , , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
BioMed Central
2012
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3439350/ https://ncbi.nlm.nih.gov/pubmed/22541333 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1186/1756-8935-5-5 |
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