ArticleThe Journal of biological chemistry2010
X-ray crystal structure of the bacterial conjugation factor PsiB, a negative regulator of RecA.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Host range and antibiotic resistance dissemination are shaped by distinct survival strategies of conjugative plasmids.Nucleic acids research · 2026Article
- Search for Origins of Anti-CRISPR Proteins by Structure Comparison.The CRISPR journal · 2023Article
- Towards a better understanding of antimicrobial resistance dissemination: what can be learnt from studying model conjugative plasmids?Military Medical Research · 2022Review
- Article
- Article
- Directed Evolution of RecA Variants with Enhanced Capacity for Conjugational Recombination.PLoS genetics · 2015Article
- Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
During bacterial conjugation, genetic material from one cell is transferred to another as single-stranded DNA. The introduction of single-stranded DNA into the recipient cell would ordinarily trigger a potentially deleterious transcriptional response called SOS, which is initiated by RecA protein filaments formed on the DNA. During F plasmid conjugation, however, the SOS response is suppressed by PsiB, an F-plasmid-encoded protein that binds and sequesters free RecA to prevent filament formation. Among the many characterized RecA modulator proteins, PsiB is unique in using sequestration as an inhibitory mechanism. We describe the crystal structure of PsiB from the Escherichia coli F plasmid. The stucture of PsiB is surprisingly similar to CapZ, a eukaryotic actin filament capping protein. Structure-directed neutralization of electronegative surfaces on PsiB abrogates RecA inhibition whereas neutralization of an electropositive surface element enhances PsiB inhibition of RecA. Together, these studies provide a first molecular view of PsiB and highlight its use as a reagent in studies of RecA activity.
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