ArticleThe EMBO journal2024
MinD-RNase E interplay controls localization of polar mRNAs in E. coli.
Article in The EMBO journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 9 citations in OpenAlex.
- Identification of proteins interacting with the N-terminal half of endoribonuclease RNase E inRNA biology · 2026Article
- Membrane Protein Insertion in Cells: Principles, Pathways, and Quality Control.Chemical reviews · 2026Review
- BR-bodies facilitate adaptive responses and survival during copper stress in Caulobacter crescentus.The Journal of biological chemistry · 2025Article
- Manipulating subcellular protein localization to enhance target protein accumulation in minicells.Journal of biological engineering · 2025Article
- Critical functions and key interactions mediated by the RNase E scaffolding domain in Pseudomonas aeruginosa.PLoS genetics · 2025Article
- Highly multiplexed spatial transcriptomics in bacteria.Science (New York, N.Y.) · 2025Article
- The membrane-targeting-sequence motif is required for exhibition of recessive resurrection in Escherichia coli RNase E.Nucleic acids research · 2025Article
- Functional diversity and molecular interactions of small membrane proteins in bacteria.microLife · 2025Review
- Highly Multiplexed Spatial Transcriptomics in Bacteria.bioRxiv : the preprint server for biology · 2024Article
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Authors and funding
9 authors at 3 institutions in 4 countries.
Funding
Abstract
The E. coli transcriptome at the cell's poles (polar transcriptome) is unique compared to the membrane and cytosol. Several factors have been suggested to mediate mRNA localization to the membrane, but the mechanism underlying polar localization of mRNAs remains unknown. Here, we combined a candidate system approach with proteomics to identify factors that mediate mRNAs localization to the cell poles. We identified the pole-to-pole oscillating protein MinD as an essential factor regulating polar mRNA localization, although it is not able to bind RNA directly. We demonstrate that RNase E, previously shown to interact with MinD, is required for proper localization of polar mRNAs. Using in silico modeling followed by experimental validation, the membrane-binding site in RNase E was found to mediate binding to MinD. Intriguingly, not only does MinD affect RNase E interaction with the membrane, but it also affects its mode of action and dynamics. Polar accumulation of RNase E in ΔminCDE cells resulted in destabilization and depletion of mRNAs from poles. Finally, we show that mislocalization of polar mRNAs may prevent polar localization of their protein products. Taken together, our findings show that the interplay between MinD and RNase E determines the composition of the polar transcriptome, thus assigning previously unknown roles for both proteins.
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Registered trials
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