ArticleMolecular cell2013
Structural basis of mRNA recognition and cleavage by toxin MazF and its regulation by antitoxin MazE in Bacillus subtilis.
Article in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 90 citations in OpenAlex.
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- Understanding the physiological role and cross-interaction network of VapBC35 toxin-antitoxin system from Mycobacterium tuberculosis.Communications biology · 2025Article
- Long Dynamic β1-β2 Loops inInternational journal of molecular sciences · 2024Article
- Discovery of Antimicrobial Agents Based on Structural and Functional Study of theAntibiotics (Basel, Switzerland) · 2024Article
- TheApplied and environmental microbiology · 2024Article
- MazEF Homologs inToxins · 2024Article
- Arbitrium communication controls phage lysogeny through non-lethal modulation of a host toxin-antitoxin defence system.Nature microbiology · 2024Article
- PemK's Arg24 is a crucial residue for PemIK toxin-antitoxin system to induce the persistence ofFrontiers in microbiology · 2024Article
- Antagonistic interactions between phage and host factors control arbitrium lysis-lysogeny decision.Nature microbiology · 2024Article
- MenT nucleotidyltransferase toxins extend tRNA acceptor stems and can be inhibited by asymmetrical antitoxin binding.Nature communications · 2023Article
- GeoBind: segmentation of nucleic acid binding interface on protein surface with geometric deep learning.Nucleic acids research · 2023Article
- Structural and mutational analysis of MazE6-operator DNA complex provide insights into autoregulation of toxin-antitoxin systems.Communications biology · 2022Article
- Functional and Biochemical Characterization of the MazEF6 Toxin-Antitoxin System of Mycobacterium tuberculosis.Journal of bacteriology · 2022Article
- Role of PemI in the Staphylococcus aureus PemIK toxin-antitoxin complex: PemI controls PemK by acting as a PemK loop mimic.Nucleic acids research · 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
- Analysis of intact prophages in genomes ofFrontiers in microbiology · 2022Article
- Not making the cut: Techniques to prevent RNA cleavage in structural studies of RNase-RNA complexes.Journal of structural biology: X · 2022Review
- Prokaryote toxin-antitoxin modules: Complex regulation of an unclear function.Protein science : a publication of the Protein Society · 2021Review
- Structural and functional analysis of theIUCrJ · 2021Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
MazF is an mRNA interferase, which, upon activation during stress conditions, cleaves mRNAs in a sequence-specific manner, resulting in cellular growth arrest. During normal growth conditions, the MazF toxin is inactivated through binding to its cognate antitoxin, MazE. How MazF specifically recognizes its mRNA target and carries out cleavage and how the formation of the MazE-MazF complex inactivates MazF remain unclear. We present crystal structures of MazF in complex with mRNA substrate and antitoxin MazE in Bacillus subtilis. The structure of MazF in complex with uncleavable UUdUACAUAA RNA substrate defines the molecular basis underlying the sequence-specific recognition of UACAU and the role of residues involved in the cleavage through site-specific mutational studies. The structure of the heterohexameric (MazF)2-(MazE)2-(MazF)2 complex in Bacillus subtilis, supplemented by mutational data, demonstrates that the positioning of the C-terminal helical segment of MazE within the RNA-binding channel of the MazF dimer prevents mRNA binding and cleavage by MazF.
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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.