ArticleThe Journal of biological chemistry2016
Substrate Recognition and Activity Regulation of the Escherichia coli mRNA Endonuclease MazF.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 56 citations in OpenAlex.
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- A bacterial toxin-antitoxin system as a native defence element against RNA phages.Biology letters · 2025Article
- Long Dynamic β1-β2 Loops inInternational journal of molecular sciences · 2024Article
- Site-specific RNA modificationRSC chemical biology · 2024Article
- Discovery of Antimicrobial Agents Based on Structural and Functional Study of theAntibiotics (Basel, Switzerland) · 2024Article
- TheApplied and environmental microbiology · 2024Article
- PemK's Arg24 is a crucial residue for PemIK toxin-antitoxin system to induce the persistence ofFrontiers in microbiology · 2024Article
- Selection of a de novo gene that can promote survival of Escherichia coli by modulating protein homeostasis pathways.Nature ecology & evolution · 2023Article
- Article
- Structural and mutational analysis of MazE6-operator DNA complex provide insights into autoregulation of toxin-antitoxin systems.Communications biology · 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
- 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
- Functional Characterization of theMicroorganisms · 2021Article
- Structural and functional analysis of theIUCrJ · 2021Article
- Functional and structural characterization of Deinococcus radiodurans R1 MazEF toxin-antitoxin system, Dr0416-Dr0417.Journal of microbiology (Seoul, Korea) · 2021Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli MazF (EcMazF) is the archetype of a large family of ribonucleases involved in bacterial stress response. The crystal structure of EcMazF in complex with a 7-nucleotide substrate mimic explains the relaxed substrate specificity of the E. coli enzyme relative to its Bacillus subtilis counterpart and provides a framework for rationalizing specificity in this enzyme family. In contrast to a conserved mode of substrate recognition and a conserved active site, regulation of enzymatic activity by the antitoxin EcMazE diverges from its B. subtilis homolog. Central in this regulation is an EcMazE-induced double conformational change as follows: a rearrangement of a crucial active site loop and a relative rotation of the two monomers in the EcMazF dimer. Both are induced by the C-terminal residues Asp-78-Trp-82 of EcMazE, which are also responsible for strong negative cooperativity in EcMazE-EcMazF binding. This situation shows unexpected parallels to the regulation of the F-plasmid CcdB activity by CcdA and further supports a common ancestor despite the different activities of the MazF and CcdB toxins. In addition, we pinpoint the origin of the lack of activity of the E24A point mutant of EcMazF in its inability to support the substrate binding-competent conformation of EcMazF.
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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.