ArticleNucleic acids research2018
Structural and kinetic insights into stimulation of RppH-dependent RNA degradation by the metabolic enzyme DapF.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed, 17 citations in OpenAlex.
- ApaH decaps NpNature chemical biology · 2026Article
- Molecular mechanism of phosphopeptide neoantigen immunogenicity.Nature communications · 2023Article
- 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
- Principles of RNA and nucleotide discrimination by the RNA processing enzyme RppH.Nucleic acids research · 2020Article
- Structures of MERS1, the 5' processing enzyme of mitochondrial mRNAs inRNA (New York, N.Y.) · 2020Article
- Diversity, versatility and complexity of bacterial gene regulation mechanisms: opportunities and drawbacks for applications in synthetic biology.FEMS microbiology reviews · 2019Review
- Noncanonical features and modifications on the 5'-end of bacterial sRNAs and mRNAs.Wiley interdisciplinary reviews. RNA · 2019Review
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Vitally important for controlling gene expression in eukaryotes and prokaryotes, the deprotection of mRNA 5' termini is governed by enzymes whose activity is modulated by interactions with ancillary factors. In Escherichia coli, 5'-end-dependent mRNA degradation begins with the generation of monophosphorylated 5' termini by the RNA pyrophosphohydrolase RppH, which can be stimulated by DapF, a diaminopimelate epimerase involved in amino acid and cell wall biosynthesis. We have determined crystal structures of RppH-DapF complexes and measured rates of RNA deprotection. These studies show that DapF potentiates RppH activity in two ways, depending on the nature of the substrate. Its stimulatory effect on the reactivity of diphosphorylated RNAs, the predominant natural substrates of RppH, requires a substrate long enough to reach DapF in the complex, while the enhanced reactivity of triphosphorylated RNAs appears to involve DapF-induced changes in RppH itself and likewise increases with substrate length. This study provides a basis for understanding the intricate relationship between cellular metabolism and mRNA decay and reveals striking parallels with the stimulation of decapping activity in eukaryotes.
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Registered trials
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