ArticleJournal of bacteriology2007
The yefM-yoeB toxin-antitoxin systems of Escherichia coli and Streptococcus pneumoniae: functional and structural correlation.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
47 citing papers in PubMed, 70 citations in OpenAlex.
- Toxin-antitoxins and sigma factors may optimize the fitness of free-living bacteria throughout the life cycle via an integrated nutrient-responsive cybernetic system.Journal of the Royal Society, Interface · 2025Review
- HiBC: a publicly available collection of bacterial strains isolated from the human gut.Nature communications · 2025Article
- Understanding the physiological role and cross-interaction network of VapBC35 toxin-antitoxin system from Mycobacterium tuberculosis.Communications biology · 2025Article
- Article
- RpoS-Regulated Genes and Phenotypes in the Phytopathogenic BacteriumInternational journal of molecular sciences · 2023Article
- Three alginate lyases provide a new gutApplied and environmental microbiology · 2023Article
- Type II bacterial toxin-antitoxins: hypotheses, facts, and the newfound plethora of the PezAT system.FEMS microbiology reviews · 2023Article
- Functional and Biochemical Characterization of the MazEF6 Toxin-Antitoxin System of Mycobacterium tuberculosis.Journal of bacteriology · 2022Article
- Combining cysteine scanning with chemical labeling to map protein-protein interactions and infer bound structure in an intrinsically disordered region.Frontiers in molecular biosciences · 2022Article
- Cellular Memory of HipA-Induced Growth Arrest: The Length of Cell Growth Arrest Becomes Shorter for Each Successive Induction.Microorganisms · 2021Article
- Interactions of theMicroorganisms · 2021Article
- Insights into Transcriptional Repression of the Homologous Toxin-Antitoxin CassettesInternational journal of molecular sciences · 2020Article
- Proteomic Characterization of Antibiotic Resistance, and Production of Antimicrobial and Virulence Factors inAntibiotics (Basel, Switzerland) · 2020Article
- Identifying a Molecular Mechanism That Imparts Species-Specific Toxicity to YoeB Toxins.Frontiers in microbiology · 2020Article
- Characterization of Two Toxin-Antitoxin Systems in Deep-SeaMarine drugs · 2019Article
- Article
- TheToxins · 2018Article
- Functional insights into the Streptococcus pneumoniae HicBA toxin-antitoxin system based on a structural study.Nucleic acids research · 2018Article
- Complete genome sequence of a commensal bacterium,Gut pathogens · 2017Article
- Structure, Biology, and Therapeutic Application of Toxin-Antitoxin Systems in Pathogenic Bacteria.Toxins · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Toxin-antitoxin loci belonging to the yefM-yoeB family are located in the chromosome or in some plasmids of several bacteria. We cloned the yefM-yoeB locus of Streptococcus pneumoniae, and these genes encode bona fide antitoxin (YefM(Spn)) and toxin (YoeB(Spn)) products. We showed that overproduction of YoeB(Spn) is toxic to Escherichia coli cells, leading to severe inhibition of cell growth and to a reduction in cell viability; this toxicity was more pronounced in an E. coli B strain than in two E. coli K-12 strains. The YoeB(Spn)-mediated toxicity could be reversed by the cognate antitoxin, YefM(Spn), but not by overproduction of the E. coli YefM antitoxin. The pneumococcal proteins were purified and were shown to interact with each other both in vitro and in vivo. Far-UV circular dichroism analyses indicated that the pneumococcal antitoxin was partially, but not totally, unfolded and was different than its E. coli counterpart. Molecular modeling showed that the toxins belonging to the family were homologous, whereas the antitoxins appeared to be specifically designed for each bacterial locus; thus, the toxin-antitoxin interactions were adapted to the different bacterial environmental conditions. Both structural features, folding and the molecular modeled structure, could explain the lack of cross-complementation between the pneumococcal and E. coli antitoxins.
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Registered trials
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.