ArticleThe Journal of biological chemistry2011
Polynucleotide phosphorylase activity may be modulated by metabolites in Escherichia coli.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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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
38 citing papers in PubMed, 61 citations in OpenAlex.
- Bacterial ribonucleoprotein bodies maintain an acidic pH environment as a mechanism of enzyme regulation.Nature communications · 2026Article
- A glycolytic intermediate gatekeeps global mRNA decay in Escherichia coli.Nature communications · 2026Article
- Ribonucleobase Oxidation and Ribonucleases Involved in the Degradation of Oxidized RNA.Biomolecules · 2026Review
- Advancement in the Methods for Isolating High Quality RNA From Mouse and Rat Intervertebral Disc.JOR spine · 2026Article
- 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
- Succinate utilisation by Salmonella is inhibited by multiple regulatory systems.PLoS genetics · 2024Article
- Human PNPase causes RNA stabilization and accumulation of R-loops in the Escherichia coli model system.Scientific reports · 2023Article
- The nsp15 Nuclease as a Good Target to Combat SARS-CoV-2: Mechanism of Action and Its Inactivation with FDA-Approved Drugs.Microorganisms · 2022Article
- Activity and Function in Human Cells of the Evolutionary Conserved Exonuclease Polynucleotide Phosphorylase.International journal of molecular sciences · 2022Review
- A cooperative PNPase-Hfq-RNA carrier complex facilitates bacterial riboregulation.Molecular cell · 2021Article
- Identification of Novel Inhibitors ofMolecules (Basel, Switzerland) · 2021Article
- SR7 - a dual-function antisense RNA fromRNA biology · 2021Article
- Identification and analysis of novel small molecule inhibitors of RNase E: Implications for antibacterial targeting and regulation of RNase E.Biochemistry and biophysics reports · 2020Article
- Bacterial ribonucleases and their roles in RNA metabolism.Critical reviews in biochemistry and molecular biology · 2019Review
- PNPase is involved in the coordination of mRNA degradation and expression in stationary phase cells of Escherichia coli.BMC genomics · 2018Article
- Novel Aspects of Polynucleotide Phosphorylase Function in Streptomyces.Antibiotics (Basel, Switzerland) · 2018Review
- Inhibition of homologous phosphorolytic ribonucleases by citrate may represent an evolutionarily conserved communicative link between RNA degradation and central metabolism.Nucleic acids research · 2017Article
- Article
- The small RNA SraG participates in PNPase homeostasis.RNA (New York, N.Y.) · 2016Article
- Dual-function sRNA encoded peptide SR1P modulates moonlighting activity of B. subtilis GapA.RNA biology · 2016Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
RNA turnover is an essential element of cellular homeostasis and response to environmental change. Whether the ribonucleases that mediate RNA turnover can respond to cellular metabolic status is an unresolved question. Here we present evidence that the Krebs cycle metabolite citrate affects the activity of Escherichia coli polynucleotide phosphorylase (PNPase) and, conversely, that cellular metabolism is affected widely by PNPase activity. An E. coli strain that requires PNPase for viability has suppressed growth in the presence of increased citrate concentration. Transcriptome analysis reveals a PNPase-mediated response to citrate, and PNPase deletion broadly impacts on the metabolome. In vitro, citrate directly binds and modulates PNPase activity, as predicted by crystallographic data. Binding of metal-chelated citrate in the active site at physiological concentrations appears to inhibit enzyme activity. However, metal-free citrate is bound at a vestigial active site, where it stimulates PNPase activity. Mutagenesis data confirmed a potential role of this vestigial site as an allosteric binding pocket that recognizes metal-free citrate. Collectively, these findings suggest that RNA degradative pathways communicate with central metabolism. This communication appears to be part of a feedback network that may contribute to global regulation of metabolism and cellular energy efficiency.
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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.