ArticleThe Journal of biological chemistry2016
Helicase Activity Plays a Crucial Role for RNase R Function in Vivo and for RNA Metabolism.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- RNA exoribonucleases in E. coli.Archives of microbiology · 2026Review
- A type II toxin-antitoxin system is responsible for the cell death at low temperature in Pseudomonas syringae Lz4W lacking RNase R.The Journal of biological chemistry · 2024Article
- RNase R vs. PNPase: selecting the best-suited exoribonuclease for environmental adaptation.Extremophiles : life under extreme conditions · 2024Review
- Exoribonuclease RNase R protects AntarcticApplied and environmental microbiology · 2023Article
- Article
- Comparative analysis of circular RNA enrichment methods.RNA biology · 2022Article
- RNase R is associated in a functional complex with the RhpA DEAD-box RNA helicase in Helicobacter pylori.Nucleic acids research · 2021Article
- Article
- An improved method for circular RNA purification using RNase R that efficiently removes linear RNAs containing G-quadruplexes or structured 3' ends.Nucleic acids research · 2019Article
- Bacterial ribonucleases and their roles in RNA metabolism.Critical reviews in biochemistry and molecular biology · 2019Review
- Role of ribosome assembly in Escherichia coli ribosomal RNA degradation.Nucleic acids research · 2018Article
- RNA helicases in RNA decay.Biochemical Society transactions · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
RNase R is a 3' to 5' hydrolytic exoribonuclease that has the unusual ability to digest highly structured RNA. The enzyme possesses an intrinsic, ATP-dependent RNA helicase activity that is essential in vitro for efficient nuclease activity against double-stranded RNA substrates, particularly at lower temperatures, with more stable RNA duplexes, and for duplexes with short 3' overhangs. Here, we inquired whether the helicase activity was also important for RNase R function in vivo and for RNA metabolism. We find that strains containing a helicase-deficient RNase R due to mutations in its ATP-binding Walker motifs exhibit growth defects at low temperatures. Most importantly, cells also lacking polynucleotide phosphorylase (PNPase), and dependent for growth on RNase R, grow extremely poorly at 34, 37, and 42 °C and do not grow at all at 31 °C. Northern analysis revealed that in these cells, fragments of 16S and 23S rRNA accumulate to high levels, leading to interference with ribosome maturation and ultimately to cell death. These findings indicate that the intrinsic helicase activity of RNase R is required for its proper functioning in vivo and for effective RNA metabolism.
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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.