Histone H4-K16 Acetylation Controls Chromatin Structure and Protein Interactions

By M. Shogren-Knaak, H. Ishii, Jian‐Min Sun, M. Pazin, J. Davie, C. Peterson. Science, 2006

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View Paper: https://www.semanticscholar.org/paper/2a89fbf0477731f32bd48c8b12bea614b2f5fea9

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Citations in the corpus

Pioneer transcription factors: establishing competence for gene expression. (2011, background): “The presence of certain histone modifications in chromatin can affect both transcription factor access (e.g., Shogren-Knaak et al. 2006; Martino et al. 2009) and transcriptional initiation (Vignali et al. 2000; Li et al. 2010).”
Regulation of nucleosome dynamics by histone modifications (2013, positive): “Indeed, in vitro experiments with the D. melanogaster ISWI chromatin remodeler indicated that its remodeling activity is inhibited by H4K12ac and H4K16ac 29,30 by interfering with the conformation of the adjacent histone H4 tail basic patch (Arg17-His18-Arg19) necessary for ISWI remodeling 31 .”
The biology of chromatin remodeling complexes. (2009, background): “Acetylation of H4K16 inhibits chromatin compaction in two ways: H4K16ac inhibits fiber formation (72, 73) and reduces, but does not abolish, ISWI remodeling activity.”
Interpreting thelanguage of histone and DNA modifications (2014, background): “It was envisioned that, in addition to histone PTMs having a direct physical effect on chromatin structure (as is the case for lysine acetylation negating the positive charge of this residue) [29], they might also function through the selective recruitment of effector proteins or readers that ‘dock’”
The world of protein acetylation. (2016, background): “disrupts the chromatin structure and results in transcription activation and maintains the euchromatin form [233].”
Histone acetyltransferase complexes: one size doesn't fit all (2007, background): “Second, H4K16 acetylation has been shown to destabilize nucleosomes and to correlate with regions of chromatin decondensatio”
Recombination centres and the orchestration of V(D)J recombination (2011, background): “In the fully activated antigen receptor locus, three principal mechanisms probably work together to free RSSs from repressive associations with nucleosomes: one, histone acetylation, which weakens the association of histone tails with DNA, loosens the chromatin fibr”