9F0O

The molecular basis and modulation of lamin-specific chromatin interaction

9F0O の概要

• エントリーDOI: 10.2210/pdb9f0o/pdb
• EMDBエントリー: 50114
• 分子名称: Histone H3.2, Histone H4, Histone H2A type 1, ... (7 entities in total)
• 機能のキーワード: nucleosome lamin a specific binding, structural protein
• 由来する生物種: Xenopus laevis (African clawed frog); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 180495.32

構造登録者

Wang, B.,Luo, Q. (登録日: 2024-04-17, 公開日: 2025-08-13, 最終更新日: 2025-10-22)

主引用文献

Wang, B.,Kronenberg-Tenga, R.,Rosti, V.,Di Patrizio Soldateschi, E.,Luo, Q.,Iannacchero, U.M.,Pinet, L.,Eibauer, M.,Boujemaa-Paterski, R.,Schuler, B.,Lanzuolo, C.,Medalia, O.
The molecular basis of lamin-specific chromatin interactions.
Nat.Struct.Mol.Biol., 32:1999-2011, 2025

PubMed Abstract: In the cell nucleus, chromatin is anchored to the nuclear lamina, a network of lamin filaments and binding proteins that underly the inner nuclear membrane. The nuclear lamina is involved in chromatin organization through the interaction of lamina-associated domains within the densely packed heterochromatin regions. Using cryo-focused ion beam milling in conjunction with cryo-electron tomography, we analyzed the distribution of nucleosomes at the lamin-chromatin interface at the nanometer scale. Depletion of lamins A and C reduced nucleosome concentration at the nuclear periphery, while B-type lamin depletion contributed to nucleosome density in proximity to the lamina but not further away. We then investigated whether specific lamins can mediate direct interactions with chromatin. Using cryo-electron microscopy, we identified a specific binding motif of the lamin A tail domain that interacts with nucleosomes, distinguishing it from the other lamin isoforms. Furthermore, we examined chromatin structure dynamics using a genome-wide analysis that revealed lamin-dependent macroscopic-scale alterations in gene expression and chromatin remodeling. Our findings provide detailed insights into the dynamic and structural interplay between lamin isoforms and chromatin, molecular interactions that shape chromatin architecture and epigenetic regulation.

PubMed: 40750945
DOI: 10.1038/s41594-025-01622-5

実験手法

ELECTRON MICROSCOPY (2.3 Å)