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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Detaylı Bibliyografya
Asıl Yazarlar: Chavez, Myrriah S, Scorgie, Jean K, Dennehey, Briana K, Noone, Seth, Tyler, Jessica K, Churchill, Mair EA
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: BioMed Central 2012
Konular:
Research
Online Erişim: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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