@article{oai:oist.repo.nii.ac.jp:00001505,
 author = {Takizawa, Yoshimasa and Ho, Cheng-Han and Tachiwana, Hiroaki and Matsunami, Hideyuki and Kobayashi, Wataru and Suzuki, Midori and Arimura, Yasuhiro and Hori, Tetsuya and Fukagawa, Tatsuo and Ohi, Melanie D. and Wolf, Matthias and Kurumizaka, Hitoshi},
 issue = {1},
 journal = {Structure},
 month = {Nov},
 note = {The histone H3 variant CENP-A is a crucial epigenetic marker for centromere specification. CENP-A forms a characteristic nucleosome and dictates the higher-order configuration of centromeric chromatin. However, little is known about how the CENP-A nucleosome affects the architecture of centromeric chromatin. In this study, we reconstituted tri-nucleosomes mimicking a centromeric nucleosome arrangement containing the CENP-A nucleosome, and determined their 3D structures by cryoelectron microscopy. The H3-CENP-A-H3 tri-nucleosomes adopt an untwisted architecture, with an outward-facing linker DNA path between nucleosomes. This is distinct from the H3-H3-H3 tri-nucleosome architecture, with an inward-facing DNA path. Intriguingly, the untwisted architecture may allow the CENP-A nucleosome to be exposed to the solvent in the condensed chromatin model. These results provide a structural basis for understanding the 3D configuration of CENP-A-containing chromatin, and may explain how centromeric proteins can specifically target the CENP-A nucleosomes buried in robust amounts of H3 nucleosomes in centromeres.},
 pages = {44--53.e4},
 title = {Cryo-EM Structures of Centromeric Tri-nucleosomes Containing a Central CENP-A Nucleosome},
 volume = {28},
 year = {2019}
}