ArticleNucleic acids research2011
Interconversion between bound and free conformations of LexA orchestrates the bacterial SOS response.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 74 citations in OpenAlex.
- Rising from the fragments: a multi-factorial regulatory framework of DNA damage response in Deinococcus radiodurans.Extremophiles : life under extreme conditions · 2026Review
- Snapshots ofiScience · 2025Article
- The LexA-RecA* structure reveals a cryptic lock-and-key mechanism for SOS activation.Nature structural & molecular biology · 2024Article
- The ClpX protease is essential for inactivating the CI master repressor and completing prophage induction in Staphylococcus aureus.Nature communications · 2023Article
- FRETing about the details: Case studies in the use of a genetically encoded fluorescent amino acid for distance-dependent energy transfer.Protein science : a publication of the Protein Society · 2023Article
- A small bacteriophage protein determines the hierarchy over co-residential jumbo phage in Bacillus thuringiensis serovar israelensis.Communications biology · 2022Article
- Genome-Wide Identification of the LexA-Mediated DNA Damage Response in Streptomyces venezuelae.Journal of bacteriology · 2022Article
- RecA and RecB: probing complexes of DNA repair proteins with mitomycin C in liveJournal of the Royal Society, Interface · 2022Article
- Growth-dependent heterogeneity in the DNA damage response in Escherichia coli.Molecular systems biology · 2022Article
- The Small DdrR Protein Directly Interacts with the UmuDAb Regulator of the Mutagenic DNA Damage Response in Acinetobacter baumannii.Journal of bacteriology · 2022Article
- Sending out an SOS - the bacterial DNA damage response.Genetics and molecular biology · 2022Article
- Transcriptional control of mycobacterial DNA damage response by sigma adaptation.Science advances · 2021Article
- Single-molecule imaging of LexA degradation in Escherichia coli elucidates regulatory mechanisms and heterogeneity of the SOS response.Nature microbiology · 2021Article
- Transcriptional profiling of the stringent response mutant strain E. coli SR reveals enhanced robustness to large-scale conditions.Microbial biotechnology · 2021Article
- Coexistence of SOS-Dependent and SOS-Independent Regulation of DNA Repair Genes in Radiation-ResistantCells · 2021Review
- Prophage Activation in the Intestine: Insights Into Functions and Possible Applications.Frontiers in microbiology · 2021Review
- Survival in Hostile Conditions: Pupylation and the Proteasome in Actinobacterial Stress Response Pathways.Frontiers in molecular biosciences · 2021Review
- Are Bacterial Persisters Dormant Cells Only?Frontiers in microbiology · 2021Review
- The Parameter-Fitness Landscape ofmSphere · 2020Article
- Two components of DNA replication-dependent LexA cleavage.The Journal of biological chemistry · 2020Article
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bacterial SOS response is essential for the maintenance of genomes, and also modulates antibiotic resistance and controls multidrug tolerance in subpopulations of cells known as persisters. In Escherichia coli, the SOS system is controlled by the interplay of the dimeric LexA transcriptional repressor with an inducer, the active RecA filament, which forms at sites of DNA damage and activates LexA for self-cleavage. Our aim was to understand how RecA filament formation at any chromosomal location can induce the SOS system, which could explain the mechanism for precise timing of induction of SOS genes. Here, we show that stimulated self-cleavage of the LexA repressor is prevented by binding to specific DNA operator targets. Distance measurements using pulse electron paramagnetic resonance spectroscopy reveal that in unbound LexA, the DNA-binding domains sample different conformations. One of these conformations is captured when LexA is bound to operator targets and this precludes interaction by RecA. Hence, the conformational flexibility of unbound LexA is the key element in establishing a co-ordinated SOS response. We show that, while LexA exhibits diverse dissociation rates from operators, it interacts extremely rapidly with DNA target sites. Modulation of LexA activity changes the occurrence of persister cells in bacterial populations.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.