ArticleThe Journal of biological chemistry2012
Structural insights into methyltransferase KsgA function in 30S ribosomal subunit biogenesis.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 83 citations in OpenAlex.
- Mechanism of 30S subunit recognition and modification by the conserved bacterial ribosomal RNA methyltransferase RsmI.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- 16S rRNA methyltransferase KsgA contributes to oxidative stress and antibiotic resistance in Pseudomonas aeruginosa.Scientific reports · 2024Article
- YjgA plays dual roles in enhancing PTC maturation.Nucleic acids research · 2024Article
- Article
- KsgA facilitates ribosomal small subunit maturation by proofreading a key structural lesion.Nature structural & molecular biology · 2023Article
- Pseudouridine Synthase RsuA Confers a Survival Advantage to Bacteria under Streptomycin Stress.Antibiotics (Basel, Switzerland) · 2023Article
- White and green striate leaves 1, predicted to encode a 16S rRNA processing protein, plays a critical role in the processing of chloroplast ribosomes in maize (Molecular breeding : new strategies in plant improvement · 2023Article
- Article
- Emerging Quantitative Biochemical, Structural, and Biophysical Methods for Studying Ribosome and Protein-RNA Complex Assembly.Biomolecules · 2023Review
- Noncatalytic regulation of 18Genes & development · 2023Article
- The nucleoplasmic phase of pre-40S formation prior to nuclear export.Nucleic acids research · 2022Article
- Decoding the Mechanism of Specific RNA Targeting by Ribosomal Methyltransferases.ACS chemical biology · 2022Article
- Protein Assistants of Small Ribosomal Subunit Biogenesis in Bacteria.Microorganisms · 2022Review
- Structural basis of successive adenosine modifications by the conserved ribosomal methyltransferase KsgA.Nucleic acids research · 2021Article
- A conserved rRNA switch is central to decoding site maturation on the small ribosomal subunit.Science advances · 2021Article
- Insights into synthesis and function of KsgA/Dim1-dependent rRNA modifications in archaea.Nucleic acids research · 2021Article
- The World of Stable Ribonucleoproteins and Its Mapping With Grad-Seq and Related Approaches.Frontiers in molecular biosciences · 2021Review
- Shared requirements for key residues in the antibiotic resistance enzymes ErmC and ErmE suggest a common mode of RNA recognition.The Journal of biological chemistry · 2020Article
- Global discovery of bacterial RNA-binding proteins by RNase-sensitive gradient profiles reports a new FinO domain protein.RNA (New York, N.Y.) · 2020Article
- Structural and catalytic roles of the human 18The Journal of biological chemistry · 2020Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The assembly of the ribosomal subunits is facilitated by ribosome biogenesis factors. The universally conserved methyltransferase KsgA modifies two adjacent adenosine residues in the 3'-terminal helix 45 of the 16 S ribosomal RNA (rRNA). KsgA recognizes its substrate adenosine residues only in the context of a near mature 30S subunit and is required for the efficient processing of the rRNA termini during ribosome biogenesis. Here, we present the cryo-EM structure of KsgA bound to a nonmethylated 30S ribosomal subunit. The structure reveals that KsgA binds to the 30S platform with the catalytic N-terminal domain interacting with substrate adenosine residues in helix 45 and the C-terminal domain making extensive contacts to helix 27 and helix 24. KsgA excludes the penultimate rRNA helix 44 from adopting its position in the mature 30S subunit, blocking the formation of the decoding site and subunit joining. We suggest that the activation of methyltransferase activity and subsequent dissociation of KsgA control conformational changes in helix 44 required for final rRNA processing and translation initiation.
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