ArticleMolecular microbiology2016
RNase E-based degradosome modulates polyadenylation of mRNAs after Rho-independent transcription terminators in Escherichia coli.
Article in Molecular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Tyrosine phosphorylation controlled poly(A) polymerase I activity regulates general stress response in bacteria.Life science alliance · 2023Article
- Dihydrolipoamide Acetyltransferase AceF Influences the Type III Secretion System and Resistance to Oxidative Stresses through RsmY/Z inMicroorganisms · 2022Article
- Regulation of mRNA decay inCritical reviews in biochemistry and molecular biology · 2022Article
- Activity and Function in Human Cells of the Evolutionary Conserved Exonuclease Polynucleotide Phosphorylase.International journal of molecular sciences · 2022Review
- Inactivation of RNase P in Escherichia coli significantly changes post-transcriptional RNA metabolism.Molecular microbiology · 2022Article
- Bacterial RNA Degradosomes: Molecular Machines under Tight Control.Trends in biochemical sciences · 2020Review
- New Insights into the Relationship between tRNA Processing and Polyadenylation in Escherichia coli.Trends in genetics : TIG · 2019Review
- Analysis of post-transcriptional RNA metabolism in prokaryotes.Methods (San Diego, Calif.) · 2019Review
- RNA search engines empower the bacterial intranet.Biochemical Society transactions · 2017Review
- Article
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6 authors at 1 institution in 1 country.
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Abstract
Here we demonstrate that the RNase E-based degradosome is required for poly(A) polymerase I (PAP I)-dependent polyadenylation after Rho-independent transcription terminators for both mono- and polycistronic transcripts. Disruption of degradosome assembly in mutants lacking the polynucleotide phosphorylase (PNPase) binding domain led to a significant increase in the level of PNPase synthesized polynucleotide tails in the rpsJ and rpsM polycistronic transcripts and the lpp monocistronic transcript. The polynucleotide tails were mostly located within the coding sequences in the degradosome mutants compared to the wild type control where the majority of the PAP I synthesized poly(A) tails were after the Rho-independent transcription terminators. For the Rho terminated metNIQ operon, the tails for all three mRNAs were predominately polynucleotide and were located within the coding sequences in both wild type and degradosome mutant strains. Furthermore, by employing a pnp-R100D point mutant that encodes a catalytically inactive PNPase protein that still forms intact degradosomes, we show that a catalytically active PNPase is required for normal mRNA polyadenylation by PAP I. Our data suggest that polyadenylation requires a functional degradosome to maintain an equilibrium between free PNPase and the PAP I polyadenylation complex.
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