ArticleNucleic acids research2013
Structural insight into LexA-RecA* interaction.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- An ancestral transmembrane transcription factor couples cell envelope regulation and the SOS response in Caulobacter crescentus.PLoS genetics · 2026Article
- Antibiotic exposure and recovery of persister states influence virulence phenotypes in Pseudomonas aeruginosa.Archives of microbiology · 2026Article
- A WYL transcriptional regulator activates the DNA damage response pathway in Acinetobacter species.Nucleic acids research · 2026Article
- Decoding the spatiotemporal heterogeneity of bacterial virulence gene expression using single-cell approaches.Frontiers in microbiology · 2026Review
- Variability in intrinsic promoter strength underlies the temporal hierarchy of the Caulobacter SOS response induction.PLoS biology · 2025Article
- Cooperative mechanisms of LexA and HtpG in the regulation of virulence gene expression inCurrent research in microbial sciences · 2025Article
- The LexA-RecA* structure reveals a cryptic lock-and-key mechanism for SOS activation.Nature structural & molecular biology · 2024Article
- Widespread prevalence of a methylation-dependent switch to activate an essential DNA damage response in bacteria.PLoS biology · 2024Article
- Modeling the Homologous Recombination Process: Methods, Successes and Challenges.International journal of molecular sciences · 2023Review
- SOS-independent bacterial DNA damage responses: diverse mechanisms, unifying function.Current opinion in microbiology · 2023Review
- 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
- Engineered RecA Constructs Reveal the Minimal SOS Activation Complex.Biochemistry · 2022Article
- A small bacteriophage protein determines the hierarchy over co-residential jumbo phage in Bacillus thuringiensis serovar israelensis.Communications biology · 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
- Non-canonical LexA proteins regulate the SOS response in the Bacteroidetes.Nucleic acids research · 2021Article
- Single-molecule imaging of LexA degradation in Escherichia coli elucidates regulatory mechanisms and heterogeneity of the SOS response.Nature microbiology · 2021Article
- Article
- Two components of DNA replication-dependent LexA cleavage.The Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RecA protein is a hallmark for the bacterial response to insults inflicted on DNA. It catalyzes the strand exchange step of homologous recombination and stimulates self-inactivation of the LexA transcriptional repressor. Importantly, by these activities, RecA contributes to the antibiotic resistance of bacteria. An original way to decrease the acquisition of antibiotic resistance would be to block RecA association with LexA. To engineer inhibitors of LexA-RecA complex formation, we have mapped the interaction area between LexA and active RecA-ssDNA filament (RecA*) and generated a three-dimensional model of the complex. The model revealed that one subunit of the LexA dimer wedges into a deep helical groove of RecA*, forming multiple interaction sites along seven consecutive RecA protomers. Based on the model, we predicted that LexA in its DNA-binding conformation also forms a complex with RecA* and that the operator DNA sterically precludes interaction with RecA*, which guides the induction of SOS gene expression. Moreover, the model shows that besides the catalytic C-terminal domain of LexA, its N-terminal DNA-binding domain also interacts with RecA*. Because all the model-based predictions have been confirmed experimentally, the presented model offers a validated insight into the critical step of the bacterial DNA damage response.
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