ArticleBioscience reports2014
The Escherichia coli major exoribonuclease RNase II is a component of the RNA degradosome.
Article in Bioscience reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- Synergistic and individual effects of RNase E, II, and R in the regulation ofApplied and environmental microbiology · 2026Article
- Quorum sensing and QsvR tightly control the transcription ofFrontiers in microbiology · 2023Article
- Zam Is a Redox-Regulated Member of the RNB-Family Required for Optimal Photosynthesis in Cyanobacteria.Microorganisms · 2022Article
- Trans-acting regulators of ribonuclease activity.Journal of microbiology (Seoul, Korea) · 2021Review
- Phase-separated bacterial ribonucleoprotein bodies organize mRNA decay.Wiley interdisciplinary reviews. RNA · 2020Review
- RNase II binds to RNase E and modulates its endoribonucleolytic activity in the cyanobacterium Anabaena PCC 7120.Nucleic acids research · 2020Article
- Bacterial RNA Degradosomes: Molecular Machines under Tight Control.Trends in biochemical sciences · 2020Review
- Examining the Protein Interactome and Subcellular Localization of RNase J2 Complexes inFrontiers in microbiology · 2019Article
- Systematic characterization of artificial small RNA-mediated inhibition of Escherichia coli growth.RNA biology · 2017Article
- Reversible acetylation on Lys501 regulates the activity of RNase II.Nucleic acids research · 2016Article
- Elucidation of the Photorhabdus temperata Genome and Generation of a Transposon Mutant Library To Identify Motility Mutants Altered in Pathogenesis.Journal of bacteriology · 2015Article
- How bacterial cells keep ribonucleases under control.FEMS microbiology reviews · 2015Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Multiprotein complexes that carry out RNA degradation and processing functions are found in cells from all domains of life. In Escherichia coli, the RNA degradosome, a four-protein complex, is required for normal RNA degradation and processing. In addition to the degradosome complex, the cell contains other ribonucleases that also play important roles in RNA processing and/or degradation. Whether the other ribonucleases are associated with the degradosome or function independently is not known. In the present work, IP (immunoprecipitation) studies from cell extracts showed that the major hydrolytic exoribonuclease RNase II is associated with the known degradosome components RNaseE (endoribonuclease E), RhlB (RNA helicase B), PNPase (polynucleotide phosphorylase) and Eno (enolase). Further evidence for the RNase II-degradosome association came from the binding of RNase II to purified RNaseE in far western affinity blot experiments. Formation of the RNase II-degradosome complex required the degradosomal proteins RhlB and PNPase as well as a C-terminal domain of RNaseE that contains binding sites for the other degradosomal proteins. This shows that the RNase II is a component of the RNA degradosome complex, a previously unrecognized association that is likely to play a role in coupling and coordinating the multiple elements of the RNA degradation pathways.
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