Current progress on structural studies of nucleosomes containing histone H3 variants
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Updated: May 15, 2026
Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
Published on: March 26, 2017
Hitoshi Kurumizaka1, Naoki Horikoshi, Hiroaki Tachiwana
1Laboratory of Structural Biology, Graduate School of Advanced Science and Engineering, Waseda University, 2-2 Wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, Japan. kurumizaka@waseda.jp
Abstract:
The nucleosome is the basic repeating unit of chromatin. During the nucleosome assembly process, DNA is wrapped around two H3-H4 dimers, followed by the inclusion of two H2A-H2B dimers. The H3-H4 dimers provide the fundamental architecture of the nucleosome. Many non-allelic variants have been found for H3, but not for H4, suggesting that the functions of chromatin domains may, at least in part, be dictated by the specific H3 variant that is incorporated. A prominent example is the centromeric H3 variant, CENP-A, which specifies the function of centromeres in chromosomes. In this review, we survey the current progress in the studies of nucleosomes containing H3 variants, and discuss their implications for the architecture and dynamics of chromatin domains.
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