ArticleFEMS microbiology letters2016
ydfD encodes a novel lytic protein in Escherichia coli.
Article in FEMS microbiology letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- A transcription factor from the cryptic Escherichia coli Rac prophage controls both phage and host operons.Nucleic acids research · 2025Article
- A Cryptic Prophage Transcription Factor Drives Phenotypic Changes via Host Gene Regulation.bioRxiv : the preprint server for biology · 2024Article
- Mechanisms of Regulation of Cryptic Prophage-Encoded Gene Products in Escherichia coli.Journal of bacteriology · 2023Article
- CRISPR-Cas Controls Cryptic Prophages.International journal of molecular sciences · 2022Article
- YdfD, a Lysis Protein of the Qin Prophage, Is a Specific Inhibitor of the IspG-Catalyzed Step in the MEP Pathway ofInternational journal of molecular sciences · 2022Article
- Genome-Wide Screening of Oxidizing Agent Resistance Genes inAntioxidants (Basel, Switzerland) · 2021Article
- The Study on Molecular Profile Changes of Pathogens via Zinc Nanocomposites Immobilization Approach.International journal of molecular sciences · 2021Article
- Cryptic-Prophage-Encoded Small Protein DicB ProtectsJournal of bacteriology · 2019Article
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Authors and funding
3 authors.
Funding
Abstract
Bacteria carry a number of genes that cause cell growth arrest or cell lysis upon expression. Notably, defective prophages retain many lysis proteins. Here, we identified a novel lytic gene, ydfD, on the Qin prophage segment of the Escherichia coli genome. YdfD lyses 99.9% of cells within 2 h of its induction. The co-expression of the upstream gene, dicB, encoding a cell division inhibitor, as well as sulA, encoding another cell division inhibitor, abolished YdfD-induced cell lysis. These results imply that YdfD-induced lysis is a cell division-dependent event. We further found that by deleting the hydrophobic 22-residue N-terminal domain, the resulting 42-residue C-terminal domain was still toxic to cause cell lysis. We propose that YdfD, associated with the cytoplasmic membrane, inhibits an essential cellular process(s).
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