ArticleStructure (London, England : 1993)2009
Structure and biological function of the RNA pyrophosphohydrolase BdRppH from Bdellovibrio bacteriovorus.
Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 42 citations in OpenAlex.
- Mycobacterium tuberculosis MutT4/RppH is an RNA pyrophosphohydrolase that forms condensate-like bodies and impacts mRNA degradation.Nucleic acids research · 2026Article
- A conserved viral RNA fold enables nuclease resistance across kingdoms of life.Nucleic acids research · 2025Article
- Visualization of mutagenic nucleotide processing byProceedings of the National Academy of Sciences of the United States of America · 2022Article
- A distinct RNA recognition mechanism governs NpProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Different tertiary interactions create the same important 3D features in a distinct flavivirus xrRNA.RNA (New York, N.Y.) · 2021Article
- The crystal structure of a Polerovirus exoribonuclease-resistant RNA shows how diverse sequences are integrated into a conserved fold.RNA (New York, N.Y.) · 2020Article
- Individual Nudix hydrolases affect diverse features of Pseudomonas aeruginosa.MicrobiologyOpen · 2020Article
- Biochemical Characterization of Yeast Xrn1.Biochemistry · 2020Article
- Principles of RNA and nucleotide discrimination by the RNA processing enzyme RppH.Nucleic acids research · 2020Article
- Short Direct Repeats in the 3' Untranslated Region Are Involved in Subgenomic Flaviviral RNA Production.Journal of virology · 2020Article
- Structures of MERS1, the 5' processing enzyme of mitochondrial mRNAs inRNA (New York, N.Y.) · 2020Article
- Regulation of mRNA Stability During Bacterial Stress Responses.Frontiers in microbiology · 2020Review
- DapF stabilizes the substrate-favoring conformation of RppH to stimulate its RNA-pyrophosphohydrolase activity in Escherichia coli.Nucleic acids research · 2018Article
- The evolution of function within the Nudix homology clan.Proteins · 2017Article
- Identification of the RNA Pyrophosphohydrolase RppH of Helicobacter pylori and Global Analysis of Its RNA Targets.The Journal of biological chemistry · 2017Article
- Zika virus produces noncoding RNAs using a multi-pseudoknot structure that confounds a cellular exonuclease.Science (New York, N.Y.) · 2016Article
- Article
- Article
- Specificity and evolutionary conservation of the Escherichia coli RNA pyrophosphohydrolase RppH.The Journal of biological chemistry · 2015Article
- 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
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7 authors at 3 institutions in 1 country.
Funding
Abstract
Until recently, the mechanism of mRNA decay in bacteria was thought to be different from that of eukaryotes. This paradigm changed with the discovery that RppH (ORF176/NudH/YgdP), an Escherichia coli enzyme that belongs to the Nudix superfamily, is an RNA pyrophosphohydrolase that initiates mRNA decay by cleaving pyrophosphate from the 5'-triphosphate. Here we report the 1.9 Angstroms resolution structure of the Nudix hydrolase BdRppH from Bdellovibrio bacteriovorus, a bacterium that feeds on other Gram-negative bacteria. Based on the structure of the enzyme alone and in complex with GTP-Mg2+, we propose a mode of RNA binding similar to that of the nuclear decapping enzyme from Xenopus laevis, X29. In additional experiments, we show that BdRppH can indeed function in vitro and in vivo as an RNA pyrophosphohydrolase. These findings set the basis for the identification of possible decapping enzymes in other bacteria.
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