Structure of the NuA4 acetyltransferase complex bound to the nucleosome
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
https://www.nature.com/articles/s41586-022-05303-x.pdf
Reference59 articles.
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2. Kayne, P. S. et al. Extremely conserved histone H4 N terminus is dispensable for growth but essential for repressing the silent mating loci in yeast. Cell 55, 27–39 (1988).
3. Dorigo, B., Schalch, T., Bystricky, K. & Richmond, T. J. Chromatin fiber folding: requirement for the histone H4 N-terminal tail. J. Mol. Biol. 327, 85–96 (2003).
4. Shogren-Knaak, M. et al. Histone H4-K16 acetylation controls chromatin structure and protein interactions. Science 311, 844–847 (2006).
5. Allard, S. et al. NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p. EMBO J. 18, 5108–5119 (1999).
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