ArticleJournal of bacteriology2010
Characterization of the RNA degradosome of Pseudoalteromonas haloplanktis: conservation of the RNase E-RhlB interaction in the gammaproteobacteria.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 38 citations in OpenAlex.
- Molecular Phylogeny of "Chemosensory Proteins" in Bacteria and Arthropods: CSP as an Extremely Ancient Gene.Journal of molecular evolution · 2026Article
- Critical functions and key interactions mediated by the RNase E scaffolding domain in Pseudomonas aeruginosa.PLoS genetics · 2025Article
- DEAD Box RNA Helicases: Biochemical Properties, Role in RNA Processing and Ribosome Biogenesis.Cell biochemistry and biophysics · 2024Review
- Article
- Phase-separated bacterial ribonucleoprotein bodies organize mRNA decay.Wiley interdisciplinary reviews. RNA · 2020Review
- Both Enolase and the DEAD-Box RNA Helicase CrhB Can Form Complexes with RNase E inApplied and environmental microbiology · 2020Article
- Bacterial RNA Degradosomes: Molecular Machines under Tight Control.Trends in biochemical sciences · 2020Review
- Article
- Detachment of the RNA degradosome from the inner membrane of Escherichia coli results in a global slowdown of mRNA degradation, proteolysis of RNase E and increased turnover of ribosome-free transcripts.Molecular microbiology · 2019Article
- RNase E and the High-Fidelity Orchestration of RNA Metabolism.Microbiology spectrum · 2018Review
- RNA helicases in RNA decay.Biochemical Society transactions · 2018Review
- Interference of a speB 5' untranslated region partial deletion with mRNA degradation in Streptococcus pyogenes.Molecular oral microbiology · 2017Article
- Elucidation of pathways of ribosomal RNA degradation: an essential role for RNase E.RNA (New York, N.Y.) · 2016Article
- The Csr system regulates genome-wide mRNA stability and transcription and thus gene expression in Escherichia coli.Scientific reports · 2016Article
- RNase E in the γ-Proteobacteria: conservation of intrinsically disordered noncatalytic region and molecular evolution of microdomains.Molecular genetics and genomics : MGG · 2015Article
- Membrane recognition and dynamics of the RNA degradosome.PLoS genetics · 2015Article
- Molecular recognition of RhlB and RNase D in the Caulobacter crescentus RNA degradosome.Nucleic acids research · 2014Article
- Initiation of mRNA decay in bacteria.Cellular and molecular life sciences : CMLS · 2014Review
- RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region.RNA (New York, N.Y.) · 2014Article
- Messenger RNA degradation in bacterial cells.Annual review of genetics · 2014Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The degradosome is a multienzyme complex involved in mRNA degradation in Escherichia coli. The essential endoribonuclease RNase E contains a large noncatalytic region necessary for protein-protein interactions with other components of the RNA degradosome. Interacting proteins include the DEAD-box RNA helicase RhlB, the glycolytic enzyme enolase, and the exoribonuclease PNPase. Pseudoalteromonas haloplanktis, a psychrotolerant gammaproteobacterium distantly related to E. coli, encodes homologs of each component of the RNA degradosome. In P. haloplanktis, RNase E associates with RhlB and PNPase but not enolase. Plasmids expressing P. haloplanktis RNase E (Ph-RNase E) can complement E. coli strains lacking E. coli RNase E (Ec-RNase E). Ph-RNase E, however, does not confer a growth advantage to E. coli at low temperature. Ph-RNase E has a heterologous protein-protein interaction with Ec-RhlB but not with Ec-enolase or Ec-PNPase. The Ph-RNase E binding sites for RhlB and PNPase were mapped by deletion analysis. The PNPase binding site is located at the C-terminal end of Ph-RNase E at the same position as that in Ec-RNase E, but the sequence of the site is not conserved. The sequence of the RhlB binding site in Ph-RNase E is related to the sequence in Ec-RNase E. Together with the heterologous interaction between Ph-RNase E and Ec-RhlB, our results suggest that the underlying structural motif for the RNase E-RhlB interaction is conserved. Since the activity of Ec-RhlB requires its physical interaction with Ec-RNase E, conservation of the underlying structural motif over a large evolutionary distance could be due to constraints involved in the control of RhlB activity.
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