ArticleScientific reports2023
RNase E biomolecular condensates stimulate PNPase activity.
Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 22 citations in OpenAlex.
- BR-bodies link RNA homeostasis to stress tolerance and intracellular fitness inbioRxiv : the preprint server for biology · 2026Article
- Ribonucleobase Oxidation and Ribonucleases Involved in the Degradation of Oxidized RNA.Biomolecules · 2026Review
- Nanoscale domains govern local diffusion and ageing within fused-in-sarcoma condensates.Nature nanotechnology · 2026Article
- Surface-Tethering Enhances Precision in Measuring Diffusion Within 3D Protein Condensates.Journal of molecular biology · 2026Article
- Defining the role of RNase E in the mycobacterial degradosome-like network.bioRxiv : the preprint server for biology · 2025Article
- BR-bodies facilitate adaptive responses and survival during copper stress in Caulobacter crescentus.The Journal of biological chemistry · 2025Article
- A multi-dentate, cooperative interaction between endo- and exo-ribonucleases within the bacterial RNA degradosome.Nucleic acids research · 2025Article
- A Perspective on the Role of Mitochondrial Biomolecular Condensates (mtBCs) in Neurodegenerative Diseases and Evolutionary Links to Bacterial BCs.International journal of molecular sciences · 2025Review
- Surface-Tethering Enhances Precision in Measuring Diffusion Within 3D Protein Condensates.bioRxiv : the preprint server for biology · 2025Article
- BR-Bodies Facilitate Adaptive Responses and Survival During Copper Stress inbioRxiv : the preprint server for biology · 2025Article
- Selective 8-oxo-rG stalling occurs in the catalytic core of polynucleotide phosphorylase (PNPase) during degradation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Biomolecular condensates as stress sensors and modulators of bacterial signaling.PLoS pathogens · 2024Review
- Macromolecular Crowding, Phase Separation, and Homeostasis in the Orchestration of Bacterial Cellular Functions.Chemical reviews · 2024Review
- Article
- The BR-body proteome contains a complex network of protein-protein and protein-RNA interactions.Cell reports · 2023Article
- The BR-body proteome contains a complex network of protein-protein and protein-RNA interactions.bioRxiv : the preprint server for biology · 2023Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Bacterial Ribonucleoprotein bodies (BR-bodies) play an essential role in organizing RNA degradation via phase separation in the cytoplasm of bacteria. BR-bodies mediate multi-step mRNA decay through the concerted activity of the endoribonuclease RNase E coupled with the 3'-5' exoribonuclease Polynucleotide Phosphorylase (PNPase). In vivo, studies indicated that the loss of PNPase recruitment into BR-bodies led to a significant build-up of RNA decay intermediates in Caulobacter crescentus. However, it remained unclear whether this is due to a lack of colocalized PNPase and RNase E within BR-bodies or whether PNPase's activity is stimulated within the BR-body. We reconstituted RNase E's C-terminal domain with PNPase towards a minimal BR-body in vitro to distinguish these possibilities. We found that PNPase's catalytic activity is accelerated when colocalized within the RNase E biomolecular condensates, partly due to scaffolding and mass action effects. In contrast, disruption of the RNase E-PNPase protein-protein interaction led to a loss of PNPase recruitment into the RNase E condensates and a loss of ribonuclease rate enhancement. We also found that RNase E's unique biomolecular condensate environment tuned PNPase's substrate specificity for poly(A) over poly(U). Intriguingly, a critical PNPase reactant, phosphate, reduces RNase E phase separation both in vitro and in vivo. This regulatory feedback ensures that under limited phosphate resources, PNPase activity is enhanced by recruitment into RNase E's biomolecular condensates.
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