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-Structure paper
タイトル | Molecular basis of FIGNL1 in dissociating RAD51 from DNA and chromatin. |
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ジャーナル・号・ページ | bioRxiv, Year 2024 |
掲載日 | 2024年7月16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 player of several crucial processes in repairing and protecting genome integrity, forms filaments ...Maintaining genome integrity is an essential and challenging process. RAD51 recombinase, the central player of several crucial processes in repairing and protecting genome integrity, forms filaments on DNA. RAD51 filaments are tightly regulated. One of these regulators is FIGNL1, that prevents persistent RAD51 foci post-damage and genotoxic chromatin association in cells. The cryogenic electron microscopy structure of FIGNL1 in complex with RAD51 reveals that the FIGNL1 forms a non-planar hexamer and RAD51 N-terminus is enclosed 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 unique mechanism for removing RAD51 from DNA and provides the molecular basis for FIGNL1 in maintaining genome stability. |
リンク | bioRxiv / PubMed:39071279 / 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 |
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キーワード | HYDROLASE / AAA / ATPase / DNA repair |