ArticleProceedings of the National Academy of Sciences of the United States of America2021
Assembly factors chaperone ribosomal RNA folding by isolating helical junctions that are prone to misfolding.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Exchange dynamics and kinetic control of gene regulation complexes.Nature reviews. Molecular cell biology · 2026Review
- Elucidating structure-function relationships in the mammalian nucleolus.Nature reviews. Molecular cell biology · 2026Review
- Nucleoplasmic checkpoint of the 40S ribosomal decoding center maturation.Cell reports · 2026Article
- Nascent RNA Folding and RNP Assembly Revealed by Single-molecule Microscopy.Journal of molecular biology · 2026Review
- Systematic mapping of small nucleolar RNA interactions in human cells.RNA biology · 2025Article
- Disassembly of unstable RNA structures by an E. coli DEAD-box chaperone accelerates ribosome assembly.Nucleic acids research · 2025Article
- Telomerase RNA structural heterogeneity in living human cells detected by DMS-MaPseq.Nature communications · 2025Article
- Ribosome Assembly and Repair.Annual review of cell and developmental biology · 2024Review
- Telomerase RNA structural heterogeneity in living human cells detected by DMS-MaPseq.bioRxiv : the preprint server for biology · 2024Article
- The kinase Rio1 and a ribosome collision-dependent decay pathway survey the integrity of 18S rRNA cleavage.PLoS biology · 2024Article
- Morphological and molecular phylogenetic characterization ofInternational journal for parasitology. Parasites and wildlife · 2023Article
- Additional principles that govern the release of pre-ribosomes from the nucleolus into the nucleoplasm in yeast.Nucleic acids research · 2023Article
- A disease associated mutant reveals how Ltv1 orchestrates RP assembly and rRNA folding of the small ribosomal subunit head.PLoS genetics · 2023Article
- A disease associated mutant reveals how Ltv1 orchestrates RP assembly and rRNA folding of the small ribosomal subunit head.bioRxiv : the preprint server for biology · 2023Article
- Quality control ensures fidelity in ribosome assembly and cellular health.The Journal of cell biology · 2023Review
- Using DMS-MaPseq to uncover the roles of DEAD-box proteins in ribosome assembly.Methods (San Diego, Calif.) · 2022Article
- The modifying enzyme Tsr3 establishes the hierarchy of Rio kinase binding in 40S ribosome assembly.RNA (New York, N.Y.) · 2022Article
- Ribosomal RNA 2'-Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Attacking a DEAD problem: The role of DEAD-box ATPases in ribosome assembly and beyond.Methods in enzymology · 2022Article
- RNA folding and functions of RNA helicases in ribosome biogenesis.RNA biology · 2022Review
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2 authors.
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Abstract
While RNAs are known to misfold, the underlying molecular causes have been mainly studied in fragments of biologically relevant larger RNAs. As these small RNAs are dominated by secondary structures, misfolding of these secondary structures remains the most-explored cause for global RNA misfolding. Conversely, how RNA chaperones function in a biological context to promote native folding beyond duplex annealing remains unknown. Here, in a combination of dimethylsulfate mutational profiling with sequencing (DMS-MaPseq), structural analyses, biochemical experiments, and yeast genetics, we show that three-helix junctions are prone to misfolding during assembly of the small ribosomal subunit in vivo. We identify ubiquitous roles for ribosome assembly factors in chaperoning their folding by preventing the formation of premature tertiary interactions, which otherwise kinetically trap misfolded junctions, thereby blocking further progress in the assembly cascade. While these protein chaperones act indirectly by binding the interaction partners of junctions, our analyses also suggest direct roles for small nucleolar RNAs (snoRNAs) in binding and chaperoning helical junctions during transcription. While these assembly factors do not utilize energy to ameliorate misfolding, our data demonstrate how their dissociation renders reversible folding steps irreversible, thereby driving native folding and assembly and setting up a timer that dictates the propensity of misfolded intermediates to escape quality control. Finally, the data demonstrate that RNA chaperones act locally on individual tertiary interactions, in contrast to protein chaperones, which globally unfold misfolded proteins.
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