Histone modifications dictate specific biological readouts
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2019, Science of the Total EnvironmentCitation Excerpt :Apart from the small globular structure, histones contain a more flexible and charged NH2-terminus named ʽhistone lysine tail (K)ʼ that protrudes from the nucleosome and contains 25–30 basic amino acids rich residues (Jenuwein and Allis, 2001). The affinity of the histones for each other, for DNA and for other chromatin associated proteins is determined by post-translational modifications of their protruding amino-terminal tails (Araki and Mimura, 2017; Jih et al., 2017; Munshi et al., 2009). The covalent modifications (acetylation, phosphorylation, methylation or ubiquitination) on the histone tail can exhibit exquisite variations which in turn regulates the chromatin remodeling and different contacts with the underlying DNA.
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