Evidence map›Paper›PMID 20962038›Full record

ArticleRNA (New York, N.Y.)2010

Modification of 16S ribosomal RNA by the KsgA methyltransferase restructures the 30S subunit to optimize ribosome function.

Hasan Demirci, Frank Murphy, Riccardo Belardinelli, Ann C Kelley, V Ramakrishnan, Steven T Gregory, Albert E Dahlberg, Gerwald Jogl

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

64 citing papers in PubMed, 97 citations in OpenAlex.

  1. Methyltransferase RsmB chaperonesScience advances · 2026
    Article
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  3. Article
  4. Genes required for survival and proliferation ofApplied and environmental microbiology · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. METTL5-mediated 18S rRNA mMolecular therapy : the journal of the American Society of Gene Therapy · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Molecular Basis of the Slow Growth ofFrontiers in cellular and infection microbiology · 2022
    Article
  18. Review
  19. Review
  20. Article

4 more citing papers are in PubMed but not listed here.

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

8 authors at 4 institutions in 3 countries.

Hasan DemirciDepartment of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, Rhode Island 02912, USA.
Frank Murphy
Riccardo Belardinelli
Ann C Kelley
V Ramakrishnan
Steven T Gregory
Albert E Dahlberg
Gerwald Jogl
Brown University · USMRC Laboratory of Molecular Biology · GBArgonne National Laboratory · USUniversità di Camerino · IT

Funding

POLYSOMES &SUBUNITS: STRUCTURE-FUNCTION RELATIONSHIPSR01GM019756 · NIGMS · BROWN UNIVERSITY · PI DAHLBERG, ALBERT E · 1985 to 2013
$8.5M
INDENTATION WITH ATOMIC FORCE MICROSCOPYF32GM019756 · NIGMS · BARNES-JEWISH HOSPITAL · PI COSTA, KEVIN D · 1998 to 1998
–
Medical Research Council MC_U105184332NIGMS NIH HHS F32 GM019756NIGMS NIH HHS GM19756NIGMS NIH HHS GM19756-37S1NIGMS NIH HHS R01 GM019756
6 · The paper itself

Abstract

All organisms incorporate post-transcriptional modifications into ribosomal RNA, influencing ribosome assembly and function in ways that are poorly understood. The most highly conserved modification is the dimethylation of two adenosines near the 3' end of the small subunit rRNA. Lack of these methylations due to deficiency in the KsgA methyltransferase stimulates translational errors during both the initiation and elongation phases of protein synthesis and confers resistance to the antibiotic kasugamycin. Here, we present the X-ray crystal structure of the Thermus thermophilus 30S ribosomal subunit lacking these dimethylations. Our data indicate that the KsgA-directed methylations facilitate structural rearrangements in order to establish a functionally optimum subunit conformation during the final stages of ribosome assembly.

Indexed as

Base SequenceCrystallography, X-RayMethylationMethyltransferasesModels, MolecularMolecular Sequence DataMutant ProteinsNucleic Acid ConformationProtein ConformationRibosomesRibosome Subunits, Small, BacterialRNA, Ribosomal, 16SStructure-Activity RelationshipThermus thermophilus16S rRNA (adenine(1518)-N(6)-adenine(1519)-N(6))-dimethyltransferaseMethyltransferasesMutant ProteinsRNA, Ribosomal, 16S

Identifiers

PMID20962038
PMCPMC2995393
OpenAlexW2127421301

What OpenQuestion holds

Textmetadata
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.