Journal
STRUCTURE
Volume 28, Issue 1, Pages 44-+Publisher
CELL PRESS
DOI: 10.1016/j.str.2019.10.016
Keywords
-
Funding
- JSPS KAKENHI [JP18H05534, JP17H01408, JP17H05013, 17H06167, 15H05972, JP 17K0731, JP19K06522]
- JST CREST [JPMJCR16G1]
- Platform Project for Supporting Drug Discovery and Life Science Research (BINDS) from AMED [JP19am0101076]
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available