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-Structure paper
タイトル | Structural basis for regulation of SOS response in bacteria. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 120, Issue 2, Page e2217493120, Year 2023 |
掲載日 | 2023年1月10日 |
著者 | Bo Gao / Liang Liang / Lu Su / Aijia Wen / Chun Zhou / Yu Feng / |
PubMed 要旨 | In response to DNA damage, bacterial RecA protein forms filaments with the assistance of DinI protein. The RecA filaments stimulate the autocleavage of LexA, the repressor of more than 50 SOS genes, ...In response to DNA damage, bacterial RecA protein forms filaments with the assistance of DinI protein. The RecA filaments stimulate the autocleavage of LexA, the repressor of more than 50 SOS genes, and activate the SOS response. During the late phase of SOS response, the RecA filaments stimulate the autocleavage of UmuD and λ repressor CI, leading to mutagenic repair and lytic cycle, respectively. Here, we determined the cryo-electron microscopy structures of RecA filaments in complex with DinI, LexA, UmuD, and λCI by helical reconstruction. The structures reveal that LexA and UmuD dimers bind in the filament groove and cleave in an intramolecular and an intermolecular manner, respectively, while λCI binds deeply in the filament groove as a monomer. Despite their distinct folds and oligomeric states, all RecA filament binders recognize the same conserved protein features in the filament groove. The SOS response in bacteria can lead to mutagenesis and antimicrobial resistance, and our study paves the way for rational drug design targeting the bacterial SOS response. |
リンク | Proc Natl Acad Sci U S A / PubMed:36598938 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 2.78 - 3.31 Å |
構造データ | EMDB-34151, PDB-7ywa: EMDB-34152, PDB-8gms: EMDB-34153, PDB-8gmt: EMDB-34154, PDB-8gmu: |
化合物 | ChemComp-MG: ChemComp-AGS: |
由来 |
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キーワード | DNA BINDING PROTEIN/DNA / SOS response / Filament / DNA repair / DNA BINDING PROTEIN-DNA COMPLEX / Helical reconstruction / RecA / UmuD / lambda repressor |