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The nucleosome represents the basic unit of chromatin, the DNA protein complex responsible for compacting the eukaryotic genome in the nucleus. Chromatin organization and functions are largely regulated at the nucleosomal level, and thus, understanding the structure, dynamics, and interactions of the nucleosome is essential to understanding the processes of gene transcription, recombination, replication, and repair. The work by Kato et al. (1) in PNAS provides a powerful tool to investigate the structural properties and interactions of the nucleosome in solution. Kato et al. (1) report resonance assignments of the methyl groups in the context of the intact nucleosome and use this information to elucidate the molecular basis of association of the high-mobility group nucleosomal-2 (HMGN2) effector. A high-resolution crystal structure of the nucleosome core particle, determined in 1997 (2), reveals a great deal about the core architecture. The nucleosome consists of an octamer of histone proteins (two copies each of H2A, H2B, H3, and H4) wrapped by ∼146 bp DNA. The crystal structure also illuminates the mechanisms underlying the formation of higher-order chromatin structure. However, it has proven difficult to investigate the structural basis of important cofactor interactions with …

Methyl fingerprinting of the nucleosome reveals the molecular mechanism of high-mobility group nucleosomal-2 (HMGN2) association