EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Resolution of transcription-induced hexasome-nucleosome complexes by Chd1 and FACT.
ジャーナル・号・ページ	Mol Cell, Vol. 84, Issue 18, Page 3423-33437.e8, Year 2024
掲載日	2024年9月19日
著者	Maik Engeholm / Johann J Roske / Elisa Oberbeckmann / Christian Dienemann / Michael Lidschreiber / Patrick Cramer / Lucas Farnung /
PubMed 要旨	To maintain the nucleosome organization of transcribed genes, ATP-dependent chromatin remodelers collaborate with histone chaperones. Here, we show that at the 5' ends of yeast genes, RNA polymerase ...To maintain the nucleosome organization of transcribed genes, ATP-dependent chromatin remodelers collaborate with histone chaperones. Here, we show that at the 5' ends of yeast genes, RNA polymerase II (RNAPII) generates hexasomes that occur directly adjacent to nucleosomes. The resulting hexasome-nucleosome complexes are then resolved by Chd1. We present two cryoelectron microscopy (cryo-EM) structures of Chd1 bound to a hexasome-nucleosome complex before and after restoration of the missing inner H2A/H2B dimer by FACT. Chd1 uniquely interacts with the complex, positioning its ATPase domain to shift the hexasome away from the nucleosome. In the absence of the inner H2A/H2B dimer, its DNA-binding domain (DBD) packs against the ATPase domain, suggesting an inhibited state. Restoration of the dimer by FACT triggers a rearrangement that displaces the DBD and stimulates Chd1 remodeling. Our results demonstrate how chromatin remodelers interact with a complex nucleosome assembly and suggest how Chd1 and FACT jointly support transcription by RNAPII.
リンク	Mol Cell / PubMed:39270644 / PubMed Central
手法	EM (単粒子)
解像度	2.8 - 6.85 Å
構造データ	51238 9gd0 EMDB-51238, PDB-9gd0: Structure of a hexasome-nucleosome complex with a dyad-to-dyad distance of 103 bp. 手法: EM (単粒子) / 解像度: 2.8 Å EMDB-51239: Nucleosome portion of SHN103, unsharpened focused refinement. 手法: EM (単粒子) / 解像度: 2.84 Å EMDB-51240: Hexasome portion of SHN103, unsharpened focused refinement. 手法: EM (単粒子) / 解像度: 3.0 Å 51241 9gd1 EMDB-51241, PDB-9gd1: Structure of Chd1 bound to a hexasome-nucleosome complex with a dyad-to-dyad distance of 103 bp. 手法: EM (単粒子) / 解像度: 4.0 Å EMDB-51242: Nucleosome portion of Chd1-bound SHN103, unsharpened focused refinement. 手法: EM (単粒子) / 解像度: 4.0 Å EMDB-51243: Hexasome portion of Chd1-bound SHN103, unsharpened focused refinement. 手法: EM (単粒子) / 解像度: 4.0 Å 51244 9gd2 EMDB-51244, PDB-9gd2: Structure of Chd1 bound to a dinucleosome with a dyad-to-dyad distance of 103 bp. 手法: EM (単粒子) / 解像度: 4.2 Å EMDB-51245: Original nucleosome portion of DN103, unsharpened focused refinement 手法: EM (単粒子) / 解像度: 4.2 Å EMDB-51246: Restored Chd1-bound nucleosome portion of DN103, unsharpened focused refinement 手法: EM (単粒子) / 解像度: 4.2 Å 51247 9gd3 EMDB-51247, PDB-9gd3: Structure of a mononucleosome bound by one copy of Chd1 with the DBD on the exit-side DNA. 手法: EM (単粒子) / 解像度: 3.0 Å EMDB-51315: Unsharpened consensus map of hexasome-nucleosome complex SHN103 手法: EM (単粒子) / 解像度: 4.25 Å EMDB-51316: Unsharpened consensus map of hexasome-nucleosome complex SHN103 bound by Chd1 手法: EM (単粒子) / 解像度: 4.9 Å EMDB-51317: Unsharpened consensus map of dinucleosome DN103 bound by Chd1 手法: EM (単粒子) / 解像度: 6.85 Å
化合物	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP / ADP, エネルギー貯蔵分子YM ChemComp-BEF: BERYLLIUM TRIFLUORIDE ION ChemComp-MG*: Unknown entry / マグネシウムジカチオン
由来	xenopus laevis (アフリカツメガエル) synthetic construct (人工物) saccharomyces cerevisiae s288c (パン酵母)
キーワード	DNA BINDING PROTEIN / chromatin / remodeling / transcription / nucleosome