Hiroaki Tachiwana

TL;DR: The structure provides the first atomic-resolution picture of the centromere-specific nucleosome, and it is revealed that CENP-A contains two extra amino acid residues in the loop 1 region, which is completely exposed to the solvent.

TL;DR: It is found that CenH3 overexpression in human cells leads to ectopic enrichment at sites of active histone turnover involving a heterotypic tetramer containing Cen H3-H4 with H3.3- H4.3 chaperone DAXX, which suggests a possible mechanism for cell resistance to anticancer treatments.

TL;DR: It is found that the nucleosomes containing human H3T is significantly unstable both in vitro and in vivo, as compared to the conventional nucleosome containing H3.1.1, and the H3t-specific residues (Met71 and Val111) are the source of the structural differences observed between H2T and H3, which may provide the basis of chromatin reorganization during spermatogenesis.

TL;DR: It is found that the deletion of the H2B or H3 N‐terminal tail affected histone–DNA interactions and substantially decreased nucleosome stability, providing important information for understanding the complex roles of histone tails in regulating chromatin structure.

TL;DR: In this article, the crystal structures of human nucleosomes containing either H3.2 or H 3.3 have been solved, and the structures were essentially the same as that of the H1.1 nucleosome.