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	Structural insights into γH2Ax containing nucleosomes.
ジャーナル・号・ページ	Nucleic Acids Res, Vol. 53, Issue 19, Year 2025
掲載日	2025年10月14日
著者	Rashmi Panigrahi / Ross Edwards / Md Touhidul Islam / Jun Lu / Ayodeji Kulepa / Tae Hwan Kim / J N Mark Glover /
PubMed 要旨	The phosphorylation of the histone variant H2AX on the nucleosome, yielding γH2AX, acts as a 'master control switch', signaling the recruitment of DNA repair factors at DNA double-stranded break ...The phosphorylation of the histone variant H2AX on the nucleosome, yielding γH2AX, acts as a 'master control switch', signaling the recruitment of DNA repair factors at DNA double-stranded break sites. This phosphorylation is recognized by BRCA1 carboxy-terminal (BRCT) domains of specific repair proteins. Using cryogenic electron microscopy (cryo-EM), we provide structural insights into diverse mononucleosome architectures and inter-nucleosomal interactions in the presence of H2AX, mimicking nucleosomes during DNA repair. We resolved three distinct stacked structures where the nucleosomal dyad axes and disk planes align parallel. The inter-nucleosomal interactions involve unique contacts mediated by the H4 N-terminal tail, exposed H2B elements, and DNA. Geometric analysis of stacking constraints, including published structures, reveals a tight distribution of rotational parameters around 0o, with the greatest variability in the translational parameter 'slide'. Our studies indicate that phosphorylation-dependent binding of BRCT domains with γH2AX nucleosomes disrupts stacking. However, no clear densities for BRCT proteins were observed, indicative of dynamic interactions. Molecular simulations replicate the stability of BRCT binding to γH2AX but do not indicate stable docked conformations of BRCT to nucleosome. We propose that BRCT recognition of γH2AX nucleosomes could contribute to chromatin decondensation during DNA damage signaling, exposing the nucleosomal acidic patch for repair factor recognition.
リンク	Nucleic Acids Res / PubMed:41123210 / PubMed Central
手法	EM (単粒子)
解像度	2.7 - 4.0 Å
構造データ	48375 9mll EMDB-48375, PDB-9mll: GammaH2AX containing nucleosomes, Parallel stack 手法: EM (単粒子) / 解像度: 3.7 Å 48376 9mln EMDB-48376, PDB-9mln: GammaH2AX containing nucleosome, Canonical (Class 1) 手法: EM (単粒子) / 解像度: 3.3 Å 48378 9mlr EMDB-48378, PDB-9mlr: GammaH2AX containing nucleosome, Half-wrapped (Class 2) 手法: EM (単粒子) / 解像度: 3.1 Å 48379 9mls EMDB-48379, PDB-9mls: GammaH2AX containing nucleosome, Extended (Class 3) 手法: EM (単粒子) / 解像度: 3.6 Å 48392 9mmk EMDB-48392, PDB-9mmk: H2AX containing nucleosome, Canonical (Class 1) 手法: EM (単粒子) / 解像度: 3.2 Å 48394 9mmm EMDB-48394, PDB-9mmm: H2AX containing nucleosomes, Parallel stack 手法: EM (単粒子) / 解像度: 4.0 Å 48395 9mmn EMDB-48395, PDB-9mmn: H2AX containing nucleosomes, Left offset stack 手法: EM (単粒子) / 解像度: 3.6 Å 48396 9mmo EMDB-48396, PDB-9mmo: H2AX containing nucleosomes, Right offset stack 手法: EM (単粒子) / 解像度: 3.9 Å 48403 9mmt EMDB-48403, PDB-9mmt: H2AX containing nucleosome, Unwrapped (Class 2) 手法: EM (単粒子) / 解像度: 3.4 Å EMDB-48406: Gamma-H2AX containing nucleosome bound to MCPH1 BRCT 手法: EM (単粒子) / 解像度: 4.0 Å EMDB-48547: gamma-H2AX containing nucleosome bound to MDC1 BRCT 手法: EM (単粒子) / 解像度: 2.7 Å
由来	homo sapiens (ヒト) synthetic construct (人工物)
キーワード	NUCLEAR PROTEIN / phosphorylation / nucleosome / nucleosome stacking