+検索条件
-Structure paper
| タイトル | Molecular basis of FIGNL1 in dissociating RAD51 from DNA and chromatin. |
|---|---|
| ジャーナル・号・ページ | Science, Vol. 387, Issue 6732, Page 426-431, Year 2025 |
| 掲載日 | 2025年1月24日 |
著者 | Alexander Carver / Tai-Yuan Yu / Luke A Yates / Travis White / Raymond Wang / Katie Lister / Maria Jasin / Xiaodong Zhang / ![]() |
| PubMed 要旨 | Maintaining genome integrity is an essential and challenging process. RAD51 recombinase, the central component of several crucial processes in repairing DNA and protecting genome integrity, forms ...Maintaining genome integrity is an essential and challenging process. RAD51 recombinase, the central component of several crucial processes in repairing DNA and protecting genome integrity, forms filaments on DNA, which are tightly regulated. One of these RAD51 regulators is FIGNL1 (fidgetin-like 1), which prevents RAD51 genotoxic chromatin association in normal cells and persistent RAD51 foci upon DNA damage. The cryogenic electron microscopy-imaged structure of FIGNL1 in complex with RAD51 reveals that FIGNL1 forms a nonplanar hexamer and encloses RAD51 N terminus in the FIGNL1 hexamer pore. Mutations in pore loop or catalytic residues of FIGNL1 render it defective in filament disassembly and are lethal in mouse embryonic stem cells. Our study reveals a distinct mechanism for removing RAD51 from bound substrates and provides the molecular basis for FIGNL1 in maintaining genome stability. |
リンク | Science / PubMed:39636933 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 3.2 Å |
| 構造データ | EMDB-18946, PDB-8r64: |
| 化合物 | ![]() ChemComp-MG: ![]() ChemComp-ATP: ![]() ChemComp-ADP: |
| 由来 |
|
キーワード | HYDROLASE / AAA / ATPase / DNA repair |
ムービー
コントローラー
構造ビューア
万見文献について



著者

リンク




homo sapiens (ヒト)
キーワード