ArticleJournal of bacteriology2012
Differential control of the rate of 5'-end-dependent mRNA degradation in Escherichia coli.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 32 citations in OpenAlex.
- Mycobacterium tuberculosis MutT4/RppH is an RNA pyrophosphohydrolase that forms condensate-like bodies and impacts mRNA degradation.Nucleic acids research · 2026Article
- N-terminal truncation of PhaCMicrobial cell factories · 2024Article
- A distinct RNA recognition mechanism governs NpProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Multifaceted impact of a nucleoside monophosphate kinase on 5'-end-dependent mRNA degradation in bacteria.Nucleic acids research · 2021Article
- Quantitative Control for Stoichiometric Protein Synthesis.Annual review of microbiology · 2021Article
- Predicting Selective RNA Processing and Stabilization Operons inFrontiers in microbiology · 2021Article
- Adaptor protein RapZ activates endoribonuclease RNase E by protein-protein interaction to cleave a small regulatory RNA.RNA (New York, N.Y.) · 2020Article
- Principles of RNA and nucleotide discrimination by the RNA processing enzyme RppH.Nucleic acids research · 2020Article
- The OPR Protein MTHI1 Controls the Expression of Two Different Subunits of ATP Synthase CFo inThe Plant cell · 2020Article
- Cross-subunit catalysis and a new phenomenon of recessive resurrection in Escherichia coli RNase E.Nucleic acids research · 2020Article
- Synonymous Mutations inFrontiers in microbiology · 2020Article
- Obstacles to Scanning by RNase E Govern Bacterial mRNA Lifetimes by Hindering Access to Distal Cleavage Sites.Molecular cell · 2019Article
- Noncanonical features and modifications on the 5'-end of bacterial sRNAs and mRNAs.Wiley interdisciplinary reviews. RNA · 2019Review
- Structural and kinetic insights into stimulation of RppH-dependent RNA degradation by the metabolic enzyme DapF.Nucleic acids research · 2018Article
- A Novel RNA Phosphorylation State Enables 5' End-Dependent Degradation in Escherichia coli.Molecular cell · 2017Article
- Identification of the RNA Pyrophosphohydrolase RppH of Helicobacter pylori and Global Analysis of Its RNA Targets.The Journal of biological chemistry · 2017Article
- The primary transcriptome of the Escherichia coli O104:H4 pAA plasmid and novel insights into its virulence gene expression and regulation.Scientific reports · 2016Article
- Distinct Requirements for 5'-Monophosphate-assisted RNA Cleavage by Escherichia coli RNase E and RNase G.The Journal of biological chemistry · 2016Article
- Structures of RNA complexes with the Escherichia coli RNA pyrophosphohydrolase RppH unveil the basis for specific 5'-end-dependent mRNA decay.The Journal of biological chemistry · 2015Article
- Specificity and evolutionary conservation of the Escherichia coli RNA pyrophosphohydrolase RppH.The Journal of biological chemistry · 2015Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Many Escherichia coli mRNAs are degraded by a 5'-end-dependent mechanism in which RppH-catalyzed conversion of the 5'-terminal triphosphate to a monophosphate triggers rapid endonucleolytic cleavage by RNase E. However, little is understood about what governs the decay rates of these transcripts. We investigated the decay of three such messages--rpsT P1, yfcZ, and ydfG--to characterize the rate-determining step in their degradation. The steady-state ratio of monophosphorylated to triphosphorylated rpsT P1 and yfcZ mRNA indicates that their decay rate is limited by cleavage of the monophosphorylated intermediate, making RNase E critical for their rapid turnover. Conversely, the decay rate of ydfG is limited by generation of the monophosphorylated intermediate; therefore, either RNase E or its less abundant paralog RNase G is sufficient for rapid ydfG degradation. Although all three transcripts are stabilized when RppH is absent, overproducing RppH does not accelerate their decay, nor does RppH overproduction appear to influence the longevity of most other messages that it targets. The failure of excess RppH to hasten rpsT P1 and yfcZ degradation despite increasing the percentage of each that is monophosphorylated is consistent with the observation that pyrophosphate removal is not the rate-limiting step in their decay. In contrast, neither the ydfG decay rate nor the fraction of ydfG transcripts that are monophosphorylated increases when the cellular concentration of RppH is raised, suggesting that, for some RppH targets, the rate of formation of the monophosphorylated intermediate is limited by an ancillary factor or by a step that precedes pyrophosphate removal.
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