Stemming the growth of pediatric gliomas through histone modification

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Abstract
A surprising theme that has emerged from sequencing the cancer genome is that mutations in genes encoding histone proteins are very common. Histones bind DNA to form bead-like structures (nucleosomes) along the DNA strand. At each nucleosome, the DNA double helix wraps around a complex of four pairs of core histone proteins (H2A, H2B, H3, and H4), spanned by a single linker protein (H1). Histones are no longer considered to be simply DNA-packaging proteins but instead are understood to be dynamic regulators of gene expression.1 Covalent modifications of histones, such as addition and removal of methyl and acetyl groups on lysine residues, induce conformational...

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