ArticleRNA biology2018
Importance of a diphosphorylated intermediate for RppH-dependent RNA degradation.
Article in RNA biology, 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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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- PAR-dCLIP: Enabling detection of RNA binding protein target transcripts bound at 5' termini through the incorporation of a decapping step.Methods in enzymology · 2024Article
- Methodologies for bacterial ribonuclease characterization using RNA-seq.FEMS microbiology reviews · 2023Review
- Regulation of mRNA decay inCritical reviews in biochemistry and molecular biology · 2022Article
- NUDT2 initiates viral RNA degradation by removal of 5'-phosphates.Nature communications · 2021Article
- Principles of RNA and nucleotide discrimination by the RNA processing enzyme RppH.Nucleic acids research · 2020Article
- Re-evaluation of Diadenosine Tetraphosphate (ApFrontiers in molecular biosciences · 2020Review
- Structural and mechanistic basis of mammalian Nudt12 RNA deNADding.Nature chemical biology · 2019Article
- 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
5 authors at 1 institution in 1 country.
Funding
Abstract
Deprotection of the 5' end appears to be a universal mechanism for triggering the degradation of mRNA in bacteria and eukaryotes. In Escherichia coli, for example, converting the 5' triphosphate of primary transcripts to a monophosphate accelerates cleavage at internal sites by the endonuclease RNase E. Previous studies have shown that the RNA pyrophosphohydrolase RppH catalyzes this transformation in vitro and generates monophosphorylated decay intermediates in vivo. Recently, we reported that purified E. coli RppH unexpectedly reacts faster with diphosphorylated than with triphosphorylated substrates. By using a novel assay, it was also determined that diphosphorylated mRNA decay intermediates are abundant in wild-type E. coli and that their fractional level increases to almost 100% for representative mRNAs in mutant cells lacking RppH. These findings indicate that the conversion of triphosphorylated to monophosphorylated RNA in E. coli is a stepwise process involving sequential phosphate removal and the transient formation of a diphosphorylated intermediate. The latter RNA phosphorylation state, which was previously unknown in bacteria, now appears to define the preferred biological substrates of E. coli RppH. The enzyme responsible for generating it remains to be identified.
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Registered trials
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