Evidence map›Paper›PMID 11805295›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

HemK, a class of protein methyl transferase with similarity to DNA methyl transferases, methylates polypeptide chain release factors, and hemK knockout induces defects in translational termination.

Kenji Nakahigashi, Naoko Kubo, Shin-ichiro Narita, Takeshi Shimaoka, Simon Goto, Taku Oshima, Hirotada Mori, Maki Maeda, Chieko Wada, Hachiro Inokuchi

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

67 citing papers in PubMed, 123 citations in OpenAlex.

  1. Article
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  3. Review
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  7. CytosolicProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Protein methylation in mitochondria.The Journal of biological chemistry · 2022
    Review
  17. Article
  18. Molecular Basis of the Slow Growth ofFrontiers in cellular and infection microbiology · 2022
    Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 1 country.

Kenji NakahigashiDepartment of Biophysics, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan. knakahig@pobox.com
Naoko Kubo
Shin-ichiro Narita
Takeshi Shimaoka
Simon Goto
Taku Oshima
Hirotada Mori
Maki Maeda
Chieko Wada
Hachiro Inokuchi
Kyoto University · JPNara Institute of Science and Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

HemK, a universally conserved protein of unknown function, has high amino acid similarity with DNA-(adenine-N6) methyl transferases (MTases). A certain mutation in hemK gene rescues the photosensitive phenotype of a ferrochelatase-deficient (hemH) mutant in Escherichia coli. A hemK knockout strain of E. coli not only suffered severe growth defects, but also showed a global shift in gene expression to anaerobic respiration, as determined by microarray analysis, and this shift may lead to the abrogation of photosensitivity by reducing the oxidative stress. Suppressor mutations that abrogated the growth defects of the hemK knockout strain were isolated and shown to be caused by a threonine to alanine change at codon 246 of polypeptide chain release factor (RF) 2, indicating that hemK plays a role in translational termination. Consistent with such a role, the hemK knockout strain showed an enhanced rate of read-through of nonsense codons and induction of transfer-mRNA-mediated tagging of proteins within the cell. By analysis of the methylation of RF1 and RF2 in vivo and in vitro, we showed that HemK methylates RF1 and RF2 in vitro within the tryptic fragment containing the conserved GGQ motif, and that hemK is required for the methylation within the same fragment of, at least, RF1 in vivo. This is an example of a protein MTase containing the DNA MTase motif and also a protein-(glutamine-N5) MTase.

Indexed as

Amino Acid SequenceAnaerobiosisbeta-GalactosidaseBinding SitesCloning, MolecularCulture MediaEscherichia coliEscherichia coli ProteinsGene DeletionGene Expression Regulation, BacterialKineticsMethylationMutation, MissenseOxidative StressOxygen ConsumptionPeptide Chain Termination, Translationalbeta-GalactosidaseCulture MediaEscherichia coli ProteinsprmC protein, E coliProtein Methyltransferases

Identifiers

PMID11805295
PMCPMC122215
OpenAlexW1990203942

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.