ArticleNucleic acids research2014
RppH-dependent pyrophosphohydrolysis of mRNAs is regulated by direct interaction with DapF in Escherichia coli.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Mycobacterium tuberculosis MutT4/RppH is an RNA pyrophosphohydrolase that forms condensate-like bodies and impacts mRNA degradation.Nucleic acids research · 2026Article
- Identification of Genetic and Environmental Factors Suppressing the Lethality and Antibiotic Susceptibility Mediated by Depletion of LptD, a Lipopolysaccharide Transport Protein.Journal of microbiology and biotechnology · 2025Article
- EF-P and its paralog EfpL (YeiP) differentially control translation of proline-containing sequences.Nature communications · 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
- The inner membrane protein LapB is required for adaptation to cold stress in an LpxC-independent manner.Journal of microbiology (Seoul, Korea) · 2021Article
- Phenotypic characterization of a conserved inner membrane protein YhcB in Escherichia coli.Journal of microbiology (Seoul, Korea) · 2020Article
- Principles of RNA and nucleotide discrimination by the RNA processing enzyme RppH.Nucleic acids research · 2020Article
- Genetic Evidence for Distinct Functions of Peptidoglycan Endopeptidases inFrontiers in microbiology · 2020Article
- YvcI fromThe Journal of biological chemistry · 2019Article
- 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
- Structural and kinetic insights into stimulation of RppH-dependent RNA degradation by the metabolic enzyme DapF.Nucleic acids research · 2018Article
- DapF stabilizes the substrate-favoring conformation of RppH to stimulate its RNA-pyrophosphohydrolase activity in Escherichia coli.Nucleic acids research · 2018Article
- Rsd balances (p)ppGpp level by stimulating the hydrolase activity of SpoT during carbon source downshift inProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- A Novel RNA Phosphorylation State Enables 5' End-Dependent Degradation in Escherichia coli.Molecular cell · 2017Article
- The general PTS component HPr determines the preference for glucose over mannitol.Scientific reports · 2017Article
- Structure and function of the bacterial decapping enzyme NudC.Nature chemical biology · 2016Article
- Structural basis of prokaryotic NAD-RNA decapping by NudC.Cell research · 2016Article
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Similar to decapping of eukaryotic mRNAs, the RppH-catalyzed conversion of 5'-terminal triphosphate to monophosphate has recently been identified as the rate-limiting step for the degradation of a subset of mRNAs in Escherichia coli. However, the regulation of RppH pyrophosphohydrolase activity is not well understood. Because the overexpression of RppH alone does not affect the decay rate of most target mRNAs, the existence of a mechanism regulating its activity has been suggested. In this study, we identified DapF, a diaminopimelate (DAP) epimerase catalyzing the stereoinversion of L,L-DAP to meso-DAP, as a regulator of RppH. DapF showed a high affinity interaction with RppH and increased its RNA pyrophosphohydrolase activity. The simultaneous overexpression of both DapF and RppH increased the decay rates of RppH target RNAs by about a factor of two. Together, our data suggest that the cellular level of DapF is a critical factor regulating the RppH-catalyzed pyrophosphate removal and the subsequent degradation of target mRNAs.
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