Evidence map›Paper›PMID 17189261›Full record

ArticleThe Journal of biological chemistry2007

Methyltransferase that modifies guanine 966 of the 16 S rRNA: functional identification and tertiary structure.

Dmitry V Lesnyak, Jerzy Osipiuk, Tatiana Skarina, Petr V Sergiev, Alexey A Bogdanov, Aled Edwards, Alexei Savchenko, Andrzej Joachimiak, Olga A Dontsova

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
–field-weighted citation impact
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

51 citing papers in PubMed.

  1. Compendium of RNA modifications for bacterial stress adaptation.Microbiology and molecular biology reviews : MMBR · 2026
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  11. Complete genome sequence of high-yield strainSynthetic and systems biotechnology · 2020
    Article
  12. Article
  13. Article
  14. Comprehensive Functional Analysis ofFrontiers in genetics · 2020
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

9 authors.

Dmitry V LesnyakDepartment of Bioinformatics and Bioengineering, Moscow State University, Moscow 119992, Russia.
Jerzy Osipiuk
Tatiana Skarina
Petr V Sergiev
Alexey A Bogdanov
Aled Edwards
Alexei Savchenko
Andrzej Joachimiak
Olga A Dontsova

Funding

The Midwest Center for Structural GenomicsU54GM074942 · NIGMS · UNIVERSITY OF CHICAGO · PI JOACHIMIAK, ANDRZEJ · 2005 to 2009
$51.0M
THE MIDWEST CENTER FOR STRUCTURAL GENOMICSP50GM062414 · NIGMS · UNIVERSITY OF CHICAGO · PI JOACHIMIAK, ANDRZEJ JOACHIMIAK · 2000 to 2004
$33.2M
NIGMS NIH HHS GM074942NIGMS NIH HHS GM62414NIGMS NIH HHS P50 GM062414NIGMS NIH HHS U54 GM074942
6 · The paper itself

Abstract

N(2)-Methylguanine 966 is located in the loop of Escherichia coli 16 S rRNA helix 31, forming a part of the P-site tRNA-binding pocket. We found yhhF to be a gene encoding for m(2)G966 specific 16 S rRNA methyltransferase. Disruption of the yhhF gene by kanamycin resistance marker leads to a loss of modification at G966. The modification could be rescued by expression of recombinant protein from the plasmid carrying the yhhF gene. Moreover, purified m(2)G966 methyltransferase, in the presence of S-adenosylomethionine (AdoMet), is able to methylate 30 S ribosomal subunits that were purified from yhhF knock-out strain in vitro. The methylation is specific for G966 base of the 16 S rRNA. The m(2)G966 methyltransferase was crystallized, and its structure has been determined and refined to 2.05A(.) The structure closely resembles RsmC rRNA methyltransferase, specific for m(2)G1207 of the 16 S rRNA. Structural comparisons and analysis of the enzyme active site suggest modes for binding AdoMet and rRNA to m(2)G966 methyltransferase. Based on the experimental data and current nomenclature the protein expressed from the yhhF gene was renamed to RsmD. A model for interaction of RsmD with ribosome has been proposed.

Indexed as

Models, MolecularEscherichia coliEscherichia coli ProteinsGuanineMethylationMethyltransferasesNucleic Acid ConformationProtein BindingProtein Structure, TertiaryRibosomesRNA, BacterialRNA, Ribosomal, 16SEscherichia coli ProteinsGuanineMethyltransferasesRNA, BacterialRNA, Ribosomal, 16SRsmD protein, E coli

Identifiers

PMID17189261
PMCPMC2885967

What OpenQuestion holds

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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.