ArticleNature communications2023
Structural insights into RNase J that plays an essential role in Mycobacterium tuberculosis RNA metabolism.
Article in Nature communications, 2023. 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, 12 citations in OpenAlex.
- The structural context of mutations in proteins predicts their effect on antibiotic resistance.eLife · 2026Article
- Recombinant Immunogens Designed by AI Epitope Prioritization Confer Protection AgainstVaccines · 2026Article
- Allosteric activation mechanism of the type VII CRISPR-Cas system.Nucleic acids research · 2026Article
- Metastable Folding of Bacillus subtilis glmS Ribozyme Modulates Turnover by RNase J1.Journal of molecular biology · 2026Article
- The GT1 domain of RNase J ensures RNA quality control through dsRNA binding in Arabidopsis plastids.Nucleic acids research · 2026Article
- The structural context of mutations in proteins predicts their effect on antibiotic resistance.bioRxiv : the preprint server for biology · 2025Article
- Insights into the fungal secretomes and their roles in the formation and stabilization of the biogenic silver nanoparticles.RSC advances · 2025Article
- New option: targeting RNase J and RNase HI in the fight against multi-drug-resistant tuberculosis.Annals of medicine and surgery (2012) · 2024Article
- The Structural and Molecular Mechanisms ofMolecules (Basel, Switzerland) · 2024Review
- Harnessing the potential of lipid nanoparticles for the delivery of chemically modified siRNA to combat hepatic adenovirus infection.Molecular therapy. Nucleic acids · 2023Article
Corrections and comments
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Authors and funding
16 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribonucleases (RNases) are responsible for RNA metabolism. RNase J, the core enzyme of the RNA degradosome, plays an essential role in global mRNA decay. Emerging evidence showed that the RNase J of Mycobacterium tuberculosis (Mtb-RNase J) could be an excellent target for treating Mtb infection. Here, crystal structures of Mtb-RNase J in apo-state and complex with the single-strand RNA reveal the conformational change upon RNA binding and hydrolysis. Mtb-RNase J forms an active homodimer through the interactions between the β-CASP and the β-lactamase domain. Knockout of RNase J slows the growth rate and changes the colony morphologies and cell length in Mycobacterium smegmatis, which is restored by RNase J complementation. Finally, RNA-seq analysis shows that the knockout strain significantly changes the expression levels of 49 genes in metabolic pathways. Thus, our current study explores the structural basis of Mtb-RNase J and might provide a promising candidate in pharmacological treatment for tuberculosis.
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