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-Structure paper
Title | Structural basis for regulation of SOS response in bacteria. |
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Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 120, Issue 2, Page e2217493120, Year 2023 |
Publish date | Jan 10, 2023 |
Authors | Bo Gao / Liang Liang / Lu Su / Aijia Wen / Chun Zhou / Yu Feng / |
PubMed Abstract | 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. |
External links | Proc Natl Acad Sci U S A / PubMed:36598938 / PubMed Central |
Methods | EM (helical sym.) |
Resolution | 2.78 - 3.31 Å |
Structure data | EMDB-34151, PDB-7ywa: EMDB-34152, PDB-8gms: EMDB-34153, PDB-8gmt: EMDB-34154, PDB-8gmu: |
Chemicals | ChemComp-MG: ChemComp-AGS: |
Source |
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Keywords | DNA BINDING PROTEIN/DNA / SOS response / Filament / DNA repair / DNA BINDING PROTEIN-DNA COMPLEX / Helical reconstruction / RecA / UmuD / lambda repressor |