7U4D

CryoEM structure of CENP-N promoted nucleosome stacks with CENP-A and 601 DNA sequence

7U4D の概要

• エントリーDOI: 10.2210/pdb7u4d/pdb
• 関連するPDBエントリー: 6C0W
• EMDBエントリー: 26332 7326
• 分子名称: Histone H3-like centromeric protein A, Histone H4, Histone H2A, ... (7 entities in total)
• 機能のキーワード: nucleosome, cenp-a, kinetochore, cenp-n, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 22
• 化学式量合計: 473200.21

構造登録者

Zhou, K.,Luger, K. (登録日: 2022-02-28, 公開日: 2022-03-30, 最終更新日: 2024-02-21)

主引用文献

Zhou, K.,Gebala, M.,Woods, D.,Sundararajan, K.,Edwards, G.,Krzizike, D.,Wereszczynski, J.,Straight, A.F.,Luger, K.
CENP-N promotes the compaction of centromeric chromatin.
Nat.Struct.Mol.Biol., 29:403-413, 2022

PubMed Abstract: The histone variant CENP-A is the epigenetic determinant for the centromere, where it is interspersed with canonical H3 to form a specialized chromatin structure that nucleates the kinetochore. How nucleosomes at the centromere arrange into higher order structures is unknown. Here we demonstrate that the human CENP-A-interacting protein CENP-N promotes the stacking of CENP-A-containing mononucleosomes and nucleosomal arrays through a previously undefined interaction between the α6 helix of CENP-N with the DNA of a neighboring nucleosome. We describe the cryo-EM structures and biophysical characterization of such CENP-N-mediated nucleosome stacks and nucleosomal arrays and demonstrate that this interaction is responsible for the formation of densely packed chromatin at the centromere in the cell. Our results provide first evidence that CENP-A, together with CENP-N, promotes specific chromatin higher order structure at the centromere.

PubMed: 35422519
DOI: 10.1038/s41594-022-00758-y

実験手法

ELECTRON MICROSCOPY (8.1 Å)