ArticleThe Journal of biological chemistry2011
Structure of the Escherichia coli antitoxin MqsA (YgiT/b3021) bound to its gene promoter reveals extensive domain rearrangements and the specificity of transcriptional regulation.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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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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Who cites it
44 citing papers in PubMed, 68 citations in OpenAlex.
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- The structural basis of hyperpromiscuity in a core combinatorial network of type II toxin-antitoxin and related phage defense systems.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Applications of toxin-antitoxin systems in synthetic biology.Engineering microbiology · 2023Review
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- Molecular basis of anti-CRISPR operon repression by Aca10.Nucleic acids research · 2022Article
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- Distinct oligomeric structures of the YoeB-YefM complex provide insights into the conditional cooperativity of type II toxin-antitoxin system.Nucleic acids research · 2020Article
- Stress Can Induce Transcription of Toxin-Antitoxin Systems without Activating Toxin.Molecular cell · 2020Article
- The autoregulator Aca2 mediates anti-CRISPR repression.Nucleic acids research · 2019Article
- Structure and DNA damage-dependent derepression mechanism for the XRE family member DG-DdrO.Nucleic acids research · 2019Article
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- Energy Transfer as A Driving Force in Nucleic Acid⁻Protein Interactions.Molecules (Basel, Switzerland) · 2019Article
- Characterization of Two Toxin-Antitoxin Systems in Deep-SeaMarine drugs · 2019Article
- A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT.Nature communications · 2019Article
- Structural Insights Into the Transcriptional Regulation of HigBA Toxin-Antitoxin System by Antitoxin HigA inFrontiers in microbiology · 2019Article
- Persistence in Phytopathogenic Bacteria: Do We Know Enough?Frontiers in microbiology · 2018Review
- Toxins of Prokaryotic Toxin-Antitoxin Systems with Sequence-Specific Endoribonuclease Activity.Toxins · 2017Review
- Crystal structure of Pseudomonas aeruginosa RsaL bound to promoter DNA reaffirms its role as a global regulator involved in quorum-sensing.Nucleic acids research · 2017Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Bacterial cultures, especially biofilms, produce a small number of persister cells, a genetically identical subpopulation of wild type cells that are metabolically dormant, exhibit multidrug tolerance, and are highly enriched in bacterial toxins. The gene most highly up-regulated in Escherichia coli persisters is mqsR, a ribonuclease toxin that, along with mqsA, forms a novel toxin·antitoxin (TA) system. Like all known TA systems, both the MqsR·MqsA complex and MqsA alone regulate their own transcription. Despite the importance of TA systems in persistence and biofilms, very little is known about how TA modules, and antitoxins in particular, bind and recognize DNA at a molecular level. Here, we report the crystal structure of MqsA bound to a 26-bp fragment from the mqsRA promoter. We show that MqsA binds DNA predominantly via its C-terminal helix-turn-helix domain, with direct binding of recognition helix residues Asn(97) and Arg(101) to the DNA major groove. Unexpectedly, the structure also revealed that the MqsA N-terminal domain interacts with the DNA phosphate backbone. This results in a more than 105° rotation of the N-terminal domains between the free and complexed states, an unprecedented rearrangement for an antitoxin. The structure also shows that MqsA bends the DNA by more than 55° in order to achieve symmetrical binding. Finally, using a combination of biochemical and NMR studies, we show that the DNA sequence specificity of MqsA is mediated by direct readout.
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