ArticlePLoS genetics2015
Membrane recognition and dynamics of the RNA degradosome.
Article in PLoS genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed, 119 citations in OpenAlex.
- Identification of proteins interacting with the N-terminal half of endoribonuclease RNase E inRNA biology · 2026Article
- Dynamic partitioning shapes the in vivo organization of theProceedings of the National Academy of Sciences of the United States of America · 2026Article
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- In vitro cleavage requirements and specificities of mycobacterial RNase E.Biochemical and biophysical research communications · 2026Article
- Dynamic partitioning shapes thebioRxiv : the preprint server for biology · 2026Article
- Rif-seq reveals Caulobacter crescentus mRNA decay is globally coordinated with transcription and translation.Cell reports · 2025Article
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- The secret life of RNA and lipids.RNA biology · 2025Review
- Glycogen phase-separation drives macromolecular rearrangement and asymmetric division in E. coli.The EMBO journal · 2025Article
- APEX2 proximity labeling of RNA in bacteria.Cell reports methods · 2025Article
- Roles of the membrane-binding motif and the C-terminal domain of RNase E in localization and diffusion ineLife · 2025Article
- A multi-dentate, cooperative interaction between endo- and exo-ribonucleases within the bacterial RNA degradosome.Nucleic acids research · 2025Article
- Single-molecule imaging reveals the roles of the membrane-binding motif and the C-terminal domain of RNase E in its localization and diffusion inbioRxiv : the preprint server for biology · 2025Article
- APEX2 proximity labeling of RNA in bacteria.bioRxiv : the preprint server for biology · 2025Article
- Glycogen phase separation drives macromolecular rearrangement and asymmetric division inbioRxiv : the preprint server for biology · 2025Article
- Formation of a membraneless compartment regulates bacterial virulence.Nature communications · 2025Article
- Effects of lipid membranes on RNA catalytic activity and stability.Biology of the cell · 2025Article
- The membrane-targeting-sequence motif is required for exhibition of recessive resurrection in Escherichia coli RNase E.Nucleic acids research · 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
- Cooperation of regulatory RNA and the RNA degradosome in transcript surveillance.Nucleic acids research · 2024Article
12 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 6 institutions in 4 countries.
Funding
Abstract
RNase E, which is the central component of the multienzyme RNA degradosome, serves as a scaffold for interaction with other enzymes involved in mRNA degradation including the DEAD-box RNA helicase RhlB. Epifluorescence microscopy under live cell conditions shows that RNase E and RhlB are membrane associated, but neither protein forms cytoskeletal-like structures as reported earlier by Taghbalout and Rothfield. We show that association of RhlB with the membrane depends on a direct protein interaction with RNase E, which is anchored to the inner cytoplasmic membrane through an MTS (Membrane Targeting Sequence). Molecular dynamics simulations show that the MTS interacts with the phospholipid bilayer by forming a stabilized amphipathic α-helix with the helical axis oriented parallel to the plane of the bilayer and hydrophobic side chains buried deep in the acyl core of the membrane. Based on the molecular dynamics simulations, we propose that the MTS freely diffuses in the membrane by a novel mechanism in which a large number of weak contacts are rapidly broken and reformed. TIRFm (Total Internal Reflection microscopy) shows that RNase E in live cells rapidly diffuses over the entire inner membrane forming short-lived foci. Diffusion could be part of a scanning mechanism facilitating substrate recognition and cooperativity. Remarkably, RNase E foci disappear and the rate of RNase E diffusion increases with rifampicin treatment. Control experiments show that the effect of rifampicin is specific to RNase E and that the effect is not a secondary consequence of the shut off of E. coli transcription. We therefore interpret the effect of rifampicin as being due to the depletion of RNA substrates for degradation. We propose a model in which formation of foci and constraints on diffusion arise from the transient clustering of RNase E into cooperative degradation bodies.
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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.