ArticleBiomolecules2020
Pseudouridine Synthase RsuA Captures an Assembly Intermediate that Is Stabilized by Ribosomal Protein S17.
Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Methyltransferase RsmB chaperonesScience advances · 2026Article
- Ribosome biogenesis in osteoarthritis: mechanisms and therapeutic potential.Journal of translational medicine · 2026Review
- Mechanistic insight into the pseudouridylation of RNA.RNA biology · 2025Review
- Epitranscriptomic modifications in programmed cell death: mechanistic insights and implications for liver diseases.Cellular & molecular biology letters · 2025Review
- Suppressor analysis links trans-translation and ribosomal protein uS7 to RluD function in Escherichia coli.Biochemical and biophysical research communications · 2024Article
- Pseudouridine Synthase RsuA Confers a Survival Advantage to Bacteria under Streptomycin Stress.Antibiotics (Basel, Switzerland) · 2023Article
- A roadmap for rRNA folding and assembly during transcription.Trends in biochemical sciences · 2021Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ribosome is a large ribonucleoprotein complex that synthesizes protein in all living organisms. Ribosome biogenesis is a complex process that requires synchronization of various cellular events, including ribosomal RNA (rRNA) transcription, ribosome assembly, and processing and post-transcriptional modification of rRNA. Ribosome biogenesis is fine-tuned with various assembly factors, possibly including nucleotide modification enzymes. Ribosomal small subunit pseudouridine synthase A (RsuA) pseudouridylates U516 of 16S helix 18. Protein RsuA is a multi-domain protein that contains the N-terminal peripheral domain, which is structurally similar to the ribosomal protein S4. Our study shows RsuA preferably binds and pseudouridylates an assembly intermediate that is stabilized by ribosomal protein S17 over the native-like complex. In addition, the N-terminal domain truncated RsuA showed that the presence of the S4-like domain is important for RsuA substrate recognition.
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Registered trials
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