ArticleNature structural & molecular biology2023
KsgA facilitates ribosomal small subunit maturation by proofreading a key structural lesion.
Article in Nature structural & molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- A conserved archaeal protein with evolutionary links to bacterial ribosome hibernation and eukaryotic energy sensing.The EMBO journal · 2026Article
- Heterogeneous reconstruction algorithms for cryoEM achieve limited particle classification accuracy on real benchmark datasets.bioRxiv : the preprint server for biology · 2026Article
- Engineered Cas9 complexes establish an experimentally grounded benchmark for heterogeneous cryoEM reconstruction methods.bioRxiv : the preprint server for biology · 2026Article
- Counting particles in cryo-electron microscopy may result in incorrect population estimates.Communications biology · 2026Article
- Capturing ribosomal structures in cellular extracts with cryoPRISM: A purification-free cryoEM approach reveals novel structural states.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Resolving structural heterogeneity in situ through cryogenic electron tomography.Current opinion in structural biology · 2026Review
- Bulk and selective autophagy cooperate to remodel a fungal proteome in response to changing nutrient availability.Cell reports · 2025Article
- YsxC is a placeholder for ribosomal protein uL2 during 50S ribosomal subunit assembly.Nucleic acids research · 2025Article
- Anti-sense oligonucleotide probing as a structural platform for studying ribonucleoprotein complex assembly.Nature communications · 2025Article
- Automated model-free analysis of cryo-EM volume ensembles with SIREn.Structure (London, England : 1993) · 2025Article
- An asymmetric nautilus-like HflK/C assembly controls FtsH proteolysis of membrane proteins.The EMBO journal · 2025Article
- Conformational landscapes of a class I ribonucleotide reductase complex during turnover reveal intrinsic dynamics and asymmetry.Nature communications · 2025Article
- Rapid structural analysis of bacterial ribosomes in situ.Communications biology · 2025Article
- Two dynamic N-terminal regions are required for function in ribosomal RNA adenine dimethylase family members.RNA (New York, N.Y.) · 2025Article
- A proteolytic AAA+ machine poised to unfold protein substrates.Nature communications · 2024Article
- Automated model-free analysis of cryo-EM volume ensembles with SIREn.bioRxiv : the preprint server for biology · 2024Article
- An asymmetric nautilus-like HflK/C assembly controls FtsH proteolysis of membrane proteins.bioRxiv : the preprint server for biology · 2024Article
- Learning structural heterogeneity from cryo-electron sub-tomograms with tomoDRGN.Nature methods · 2024Article
- Contribution of an alternative 16S rRNA helix to biogenesis of the 30S subunit of the ribosome.RNA (New York, N.Y.) · 2024Article
- Critical steps in the assembly process of the bacterial 50S ribosomal subunit.Nucleic acids research · 2024Review
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5 authors.
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Abstract
Ribosome assembly is orchestrated by many assembly factors, including ribosomal RNA methyltransferases, whose precise role is poorly understood. Here, we leverage the power of cryo-EM and machine learning to discover that the E. coli methyltransferase KsgA performs a 'proofreading' function in the assembly of the small ribosomal subunit by recognizing and partially disassembling particles that have matured but are not competent for translation. We propose that this activity allows inactive particles an opportunity to reassemble into an active state, thereby increasing overall assembly fidelity. Detailed structural quantifications in our datasets additionally enabled the expansion of the Nomura assembly map to highlight rRNA helix and r-protein interdependencies, detailing how the binding and docking of these elements are tightly coupled. These results have wide-ranging implications for our understanding of the quality-control mechanisms governing ribosome biogenesis and showcase the power of heterogeneity analysis in cryo-EM to unveil functionally relevant information in biological systems.
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