ArticleNucleic acids research2020
Distinct oligomeric structures of the YoeB-YefM complex provide insights into the conditional cooperativity of type II toxin-antitoxin system.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Phosphorylation of PfiA modulates Pf4 phage production through PfiA/PfiT stoichiometric reconfiguration inScience advances · 2026Article
- Type II Toxin-Antitoxin Systems inInfection and drug resistance · 2025Review
- Type II bacterial toxin-antitoxins: hypotheses, facts, and the newfound plethora of the PezAT system.FEMS microbiology reviews · 2023Article
- Dynamics-Based Regulatory Switches of Type II Antitoxins: Insights into New Antimicrobial Discovery.Antibiotics (Basel, Switzerland) · 2023Article
- Structural Analysis of Ino2p/Ino4p Mutual Interactions and Their Binding Interface with Promoter DNA.International journal of molecular sciences · 2022Article
- Structural and functional determinants inferred from deep mutational scans.Protein science : a publication of the Protein Society · 2022Article
- Evolving complex insulation.Nature chemical biology · 2021Article
- Auxiliary interfaces support the evolution of specific toxin-antitoxin pairing.Nature chemical biology · 2021Article
- Entropic pressure controls the oligomerization of the Vibrio cholerae ParD2 antitoxin.Acta crystallographica. Section D, Structural biology · 2021Article
- Prokaryote toxin-antitoxin modules: Complex regulation of an unclear function.Protein science : a publication of the Protein Society · 2021Review
- Interactions of theMicroorganisms · 2021Article
- Article
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8 authors.
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Abstract
YoeB-YefM, the widespread type II toxin-antitoxin (TA) module, binds to its own promoter to autoregulate its transcription: repress or induce transcription under normal or stress conditions, respectively. It remains unclear how YoeB-YefM regulates its transcription depending on the YoeB to YefM TA ratio. We find that YoeB-YefM complex from S.aureus exists as two distinct oligomeric assemblies: heterotetramer (YoeB-YefM2-YoeB) and heterohexamer (YoeB-YefM2-YefM2-YoeB) with low and high DNA-binding affinities, respectively. Structures of the heterotetramer alone and heterohexamer bound to promoter DNA reveals that YefM C-terminal domain undergoes disorder to order transition upon YoeB binding, which allosterically affects the conformation of N-terminal DNA-binding domain. At TA ratio of 1:2, unsaturated binding of YoeB to the C-terminal regions of YefM dimer forms an optimal heterohexamer for DNA binding, and two YefM dimers with N-terminal domains dock into the adjacent major grooves of DNA to specifically recognize the 5'-TTGTACAN6AGTACAA-3' palindromic sequence, resulting in transcriptional repression. In contrast, at TA ratio of 1:1, binding of two additional YoeB molecules onto the heterohexamer induces the completely ordered conformation of YefM and disassembles the heterohexamer into two heterotetramers, which are unable to bind the promoter DNA optimally due to steric clashes, hence derepresses TA operon transcription.
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