Evidence map›Paper›PMID 34086932›Full record

ArticleNucleic acids research2021

Structural basis of successive adenosine modifications by the conserved ribosomal methyltransferase KsgA.

Niklas C Stephan, Anne B Ries, Daniel Boehringer, Nenad Ban

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.0field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 28 citations in OpenAlex.

  1. 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 · 2026
    Article
  2. Mechanistic insights into 50Science advances · 2025
    Article
  3. Article
  4. Article
  5. Complete list of canonical post-transcriptional modifications in thebioRxiv : the preprint server for biology · 2024
    Article
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  8. 30S subunit recognition and G1405 modification by the aminoglycoside-resistance 16S ribosomal RNA methyltransferase RmtC.Proceedings of the National Academy of Sciences of the United States of America · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Niklas C StephanInstitute of Molecular Biology and Biophysics, ETH Zurich (Swiss Federal Institute of Technology), Zürich, Otto-Stern-Weg 5, Zürich 8093, Switzerland.
Anne B RiesInstitute of Molecular Biology and Biophysics, ETH Zurich (Swiss Federal Institute of Technology), Zürich, Otto-Stern-Weg 5, Zürich 8093, Switzerland.ORCID 0000-0003-1079-9197
Daniel BoehringerInstitute of Molecular Biology and Biophysics, ETH Zurich (Swiss Federal Institute of Technology), Zürich, Otto-Stern-Weg 5, Zürich 8093, Switzerland.
Nenad BanInstitute of Molecular Biology and Biophysics, ETH Zurich (Swiss Federal Institute of Technology), Zürich, Otto-Stern-Weg 5, Zürich 8093, Switzerland.ORCID 0000-0002-9527-210X
ETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biogenesis of ribosomal subunits involves enzymatic modifications of rRNA that fine-tune functionally important regions. The universally conserved prokaryotic dimethyltransferase KsgA sequentially modifies two universally conserved adenosine residues in helix 45 of the small ribosomal subunit rRNA, which is in proximity of the decoding site. Here we present the cryo-EM structure of Escherichia coli KsgA bound to an E. coli 30S at a resolution of 3.1 Å. The high-resolution structure reveals how KsgA recognizes immature rRNA and binds helix 45 in a conformation where one of the substrate nucleotides is flipped-out into the active site. We suggest that successive processing of two adjacent nucleotides involves base-flipping of the rRNA, which allows modification of the second substrate nucleotide without dissociation of the enzyme. Since KsgA is homologous to the essential eukaryotic methyltransferase Dim1 involved in 40S maturation, these results have also implications for understanding eukaryotic ribosome maturation.

Indexed as

AdenosineCryoelectron MicroscopyEscherichia coliMethyltransferasesModels, MolecularProtein ConformationRibosome Subunits, Small, BacterialSubstrate Specificity16S rRNA (adenine(1518)-N(6)-adenine(1519)-N(6))-dimethyltransferaseAdenosineMethyltransferases

Identifiers

PMID34086932
PMCPMC8216452
OpenAlexW3164377177

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.