ArticleNucleic acids research2017
Protein-only RNase P function in Escherichia coli: viability, processing defects and differences between PRORP isoenzymes.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Bacterial/archaeal protein-only RNase P: complementation inRNA (New York, N.Y.) · 2025Article
- Genome-Wide Computational Prediction and Analysis of Noncoding RNAs inMicroorganisms · 2024Article
- Discovery, structure, mechanisms, and evolution of protein-only RNase P enzymes.The Journal of biological chemistry · 2024Review
- The previously uncharacterized RnpM (YlxR) protein modulates the activity of ribonuclease P in Bacillus subtilis in vitro.Nucleic acids research · 2024Article
- Characterization of RNA-based and protein-only RNases P from bacteria encoding both enzyme types.RNA (New York, N.Y.) · 2023Article
- Synthetic riboswitches for the analysis of tRNA processing by eukaryotic RNase P enzymes.RNA (New York, N.Y.) · 2022Article
- Involvement ofInternational journal of molecular sciences · 2022Article
- Inactivation of RNase P in Escherichia coli significantly changes post-transcriptional RNA metabolism.Molecular microbiology · 2022Article
- Generation of pre-tRNAs from polycistronic operons is the essential function of RNase P in Escherichia coli.Nucleic acids research · 2020Article
- The cellular landscape of mid-size noncoding RNA.Wiley interdisciplinary reviews. RNA · 2019Review
- Bacterial ribonucleases and their roles in RNA metabolism.Critical reviews in biochemistry and molecular biology · 2019Review
- Distributive enzyme binding controlled by local RNA context results in 3' to 5' directional processing of dicistronic tRNA precursors by Escherichia coli ribonuclease P.Nucleic acids research · 2019Article
- Biochemical Studies Provide Insights into the Necessity for Multiple Arabidopsis thaliana Protein-Only RNase P Isoenzymes.Journal of molecular biology · 2019Article
- Chance and necessity in the evolution of RNase P.RNA (New York, N.Y.) · 2018Article
- Minimal and RNA-free RNase P inProceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RNase P family comprises structurally diverse endoribonucleases ranging from complex ribonucleoproteins to single polypeptides. We show that the organellar (AtPRORP1) and the two nuclear (AtPRORP2,3) single-polypeptide RNase P isoenzymes from Arabidopsis thaliana confer viability to Escherichia coli cells with a lethal knockdown of its endogenous RNA-based RNase P. RNA-Seq revealed that AtPRORP1, compared with bacterial RNase P or AtPRORP3, cleaves several precursor tRNAs (pre-tRNAs) aberrantly in E. coli. Aberrant cleavage by AtPRORP1 was mainly observed for pre-tRNAs that can form short acceptor-stem extensions involving G:C base pairs, including tRNAAsp(GUC), tRNASer(CGA) and tRNAHis. However, both AtPRORP1 and 3 were defective in processing of E. coli pre-tRNASec carrying an acceptor stem expanded by three G:C base pairs. Instead, pre-tRNASec was degraded, suggesting that tRNASec is dispensable for E. coli under laboratory conditions. AtPRORP1, 2 and 3 are also essentially unable to process the primary transcript of 4.5S RNA, a hairpin-like non-tRNA substrate processed by E. coli RNase P, indicating that PRORP enzymes have a narrower, more tRNA-centric substrate spectrum than bacterial RNA-based RNase P enzymes. The cells' viability also suggests that the essential function of the signal recognition particle can be maintained with a 5΄-extended 4.5S RNA.
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