ArticleMolecular microbiology2022
Escherichia coli SymE is a DNA-binding protein that can condense the nucleoid.
Article in Molecular microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- Adaptative and ancient co-evolution of integrons withMicrobial genomics · 2025Article
- Escherichia coli type I toxin TisB exclusively controls proton depolarization following antibiotic induced DNA damage.Scientific reports · 2025Article
- Identification, characterization and classification of prokaryotic nucleoid-associated proteins.Molecular microbiology · 2025Review
- Type I toxin-antitoxin systems in bacteria: from regulation to biological functions.EcoSal Plus · 2024Review
- A Cryptic Prophage Transcription Factor Drives Phenotypic Changes via Host Gene Regulation.bioRxiv : the preprint server for biology · 2024Article
- Article
- Effect of Divalent Metal Ions on the Ribonuclease Activity of the Toxin Molecule HP0894 fromLife (Basel, Switzerland) · 2024Article
- Core defense hotspots within Pseudomonas aeruginosa are a consistent and rich source of anti-phage defense systems.Nucleic acids research · 2023Article
- High Abundance of Transcription Regulators Compacts the Nucleoid in Escherichia coli.Journal of bacteriology · 2022Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Type I toxin-antitoxin (TA) systems typically consist of a protein toxin that imbeds in the inner membrane where it can oligomerize and form pores that change membrane permeability, and an RNA antitoxin that interacts directly with toxin mRNA to inhibit its translation. In Escherichia coli, symE/symR is annotated as a type I TA system with a non-canonical toxin. SymE was initially suggested to be an endoribonuclease, but has predicted structural similarity to DNA binding proteins. To better understand SymE function, we used RNA-seq to examine cells ectopically producing it. Although SymE drives major changes in gene expression, we do not find strong evidence of endoribonucleolytic activity. Instead, our biochemical and cell biological studies indicate that SymE binds DNA. We demonstrate that the toxicity of symE overexpression likely stems from its ability to drive severe nucleoid condensation, which disrupts DNA and RNA synthesis and leads to DNA damage, similar to the effects of overproducing the nucleoid-associated protein H-NS. Collectively, our results suggest that SymE represents a new class of nucleoid-associated proteins that is widely distributed in bacteria.
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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.