ArticleNucleic acids research2021
Escherichia coli RNase E can efficiently replace RNase Y in Bacillus subtilis.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- RNase Y mediates posttranscriptional control of the virulence-associated CncR1 small-RNA iniScience · 2025Article
- Recent progress in proteins regulating the germination ofJournal of bacteriology · 2025Review
- In Vivo Quantification of Surfactin Nonribosomal Peptide Synthetase Complexes inMicroorganisms · 2024Article
- Membrane Localization of RNase Y Is Important for Global Gene Expression inInternational journal of molecular sciences · 2024Article
- Critical factors for precise and efficient RNA cleavage by RNase Y in Staphylococcus aureus.PLoS genetics · 2024Article
- Processing and decay of 6S-1 and 6S-2 RNAs inRNA (New York, N.Y.) · 2023Article
- Shutdown of multidrug transporterRNA (New York, N.Y.) · 2023Article
- Stem-loop structures control mRNA processing of the cellulosomal cip-cel operon in Ruminiclostridium cellulolyticum.Biotechnology for biofuels and bioproducts · 2023Article
- RNase Y Autoregulates Its Synthesis inMicroorganisms · 2023Article
- Structural Insights into the Dimeric Form ofBiomolecules · 2022Article
- Transcriptome-wide in vivo mapping of cleavage sites for the compact cyanobacterial ribonuclease E reveals insights into its function and substrate recognition.Nucleic acids research · 2021Article
- Quasi-essentiality of RNase Y in Bacillus subtilis is caused by its critical role in the control of mRNA homeostasis.Nucleic acids research · 2021Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RNase Y and RNase E are disparate endoribonucleases that govern global mRNA turnover/processing in the two evolutionary distant bacteria Bacillus subtilis and Escherichia coli, respectively. The two enzymes share a similar in vitro cleavage specificity and subcellular localization. To evaluate the potential equivalence in biological function between the two enzymes in vivo we analyzed whether and to what extent RNase E is able to replace RNase Y in B. subtilis. Full-length RNase E almost completely restores wild type growth of the rny mutant. This is matched by a surprising reversal of transcript profiles both of individual genes and on a genome-wide scale. The single most important parameter to efficient complementation is the requirement for RNase E to localize to the inner membrane while truncation of the C-terminal sequences corresponding to the degradosome scaffold has only a minor effect. We also compared the in vitro cleavage activity for the major decay initiating ribonucleases Y, E and J and show that no conclusions can be drawn with respect to their activity in vivo. Our data confirm the notion that RNase Y and RNase E have evolved through convergent evolution towards a low specificity endonuclease activity universally important in bacteria.
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