ArticleMolecular cell2018
α-Proteobacterial RNA Degradosomes Assemble Liquid-Liquid Phase-Separated RNP Bodies.
Article in Molecular cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 130 papers.
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Who cites it
130 citing papers in PubMed, 232 citations in OpenAlex.
- Article
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- Distinct Spatial Organisation of Rho and RNA Polymerase in Salmonella Cells.Molecular microbiology · 2026Article
- Bacterial ribonucleoprotein bodies maintain an acidic pH environment as a mechanism of enzyme regulation.Nature communications · 2026Article
- Fast assembly and in vivo coalescence of ParBF biocondensates involved in bacterial DNA partition.Nucleic acids research · 2026Article
- RNase E resolves toxic condensates by counteracting phase separation of Type II RhlB helicases.Nucleic acids research · 2026Article
- Bottom-up reconstruction of synthetic pyrenoids provides insights into the mechanisms and evolution of carbon concentration by EPYC1 proteins.Nature plants · 2026Article
- Review
- Liquid-liquid phase separation and a phage-encoded inhibitor cooperatively drive transcriptional transition during phage SPO1 infection.Nucleic acids research · 2026Article
- BR-bodies link RNA homeostasis to stress tolerance and intracellular fitness inbioRxiv : the preprint server for biology · 2026Article
- Spatial and genetic constraints govern transcription-translation coupling and mRNA degradation in bacteria.Nature microbiology · 2026Article
- Short autoinhibitory sequences control phase separation of an essential bacterial transcription termination factor.The EMBO journal · 2026Article
- Review
- Identifying Subcellular Structure Components in Escherichia Coli by Crosslinking and SEC-MS.Proteomics · 2026Article
- Polyphosphate modulates the stress-responsive formation of functional RNA-protein condensates in bacteria and mammalian cells.PLoS biology · 2026Article
- Mycobacterium tuberculosis MutT4/RppH is an RNA pyrophosphohydrolase that forms condensate-like bodies and impacts mRNA degradation.Nucleic acids research · 2026Article
- DEAD-box ATPase-marked condensates coordinate compartmentalized translation and antibiotic persistence.Science advances · 2026Article
- Rif-seq reveals Caulobacter crescentus mRNA decay is globally coordinated with transcription and translation.Cell reports · 2025Article
- Article
- APEX2 proximity labeling of RNA in bacteria.Cell reports methods · 2025Article
70 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Ribonucleoprotein (RNP) granules play an important role in organizing eukaryotic mRNA metabolism via liquid-liquid phase separation (LLPS) of mRNA decay factors into membrane-less organelles in the cytoplasm. Here we show that the bacterium Caulobacter crescentus Ribonuclease (RNase) E assembles RNP LLPS condensates that we term bacterial RNP-bodies (BR-bodies), similar to eukaryotic P-bodies and stress granules. RNase E requires RNA to assemble a BR-body, and disassembly requires RNA cleavage, suggesting BR-bodies provide localized sites of RNA degradation. The unstructured C-terminal domain of RNase E is both necessary and sufficient to assemble the core of the BR-body, is functionally conserved in related α-proteobacteria, and influences mRNA degradation. BR-bodies are rapidly induced under cellular stresses and provide enhanced cell growth under stress. To our knowledge, Caulobacter RNase E is the first bacterial protein identified that forms LLPS condensates, providing an effective strategy for subcellular organization in cells lacking membrane-bound compartments.
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