Evidence map›Paper›PMID 27789694›Full record

ArticleNucleic acids research2017

The RNA ligase RtcB reverses MazF-induced ribosome heterogeneity in Escherichia coli.

Hannes Temmel, Christian Müller, Martina Sauert, Oliver Vesper, Ariela Reiss, Johannes Popow, Javier Martinez, Isabella Moll

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

39 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Enzymology of the metazoan tRNA ligase complex: a lifetime in cycles.Cellular and molecular life sciences : CMLS · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Lessons from RatA: Why the Basics in Molecular Biology Are Still Crucial!International journal of molecular sciences · 2025
    Article
  8. Article
  9. Ribosome Assembly and Repair.Annual review of cell and developmental biology · 2024
    Review
  10. Article
  11. Article
  12. Insights into the structure and function of the RNA ligase RtcB.Cellular and molecular life sciences : CMLS · 2023
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Transcriptome Analysis ofInternational journal of environmental research and public health · 2022
    Article
  18. Article
  19. International journal of molecular sciences · 2022
    Article
  20. Review
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 1 country.

Hannes TemmelMax F. Perutz Laboratories, Center for Molecular Biology, Department of Microbiology, Immunobiology and Genetics, University of Vienna, Vienna Biocenter (VBC), Dr Bohr-Gasse 9/4, A-1030 Vienna, Austria.
Christian MüllerMax F. Perutz Laboratories, Center for Molecular Biology, Department of Microbiology, Immunobiology and Genetics, University of Vienna, Vienna Biocenter (VBC), Dr Bohr-Gasse 9/4, A-1030 Vienna, Austria.
Martina SauertMax F. Perutz Laboratories, Center for Molecular Biology, Department of Microbiology, Immunobiology and Genetics, University of Vienna, Vienna Biocenter (VBC), Dr Bohr-Gasse 9/4, A-1030 Vienna, Austria.
Oliver VesperMax F. Perutz Laboratories, Center for Molecular Biology, Department of Microbiology, Immunobiology and Genetics, University of Vienna, Vienna Biocenter (VBC), Dr Bohr-Gasse 9/4, A-1030 Vienna, Austria.
Ariela ReissInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna Biocenter (VBC), A-1030 Vienna, Austria and Max F. Perutz Laboratories, Department of Medical Biochemistry, Medical University of Vienna, Vienna Biocenter (VBC), Dr Bohr-Gasse 9/4, A-1030 Vienna, Austria.
Johannes PopowInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna Biocenter (VBC), A-1030 Vienna, Austria and Max F. Perutz Laboratories, Department of Medical Biochemistry, Medical University of Vienna, Vienna Biocenter (VBC), Dr Bohr-Gasse 9/4, A-1030 Vienna, Austria.
Javier MartinezInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna Biocenter (VBC), A-1030 Vienna, Austria and Max F. Perutz Laboratories, Department of Medical Biochemistry, Medical University of Vienna, Vienna Biocenter (VBC), Dr Bohr-Gasse 9/4, A-1030 Vienna, Austria.
Isabella MollMax F. Perutz Laboratories, Center for Molecular Biology, Department of Microbiology, Immunobiology and Genetics, University of Vienna, Vienna Biocenter (VBC), Dr Bohr-Gasse 9/4, A-1030 Vienna, Austria.
University of Vienna · ATVienna Biocenter · ATAustrian Academy of Sciences · ATInstitute of Molecular Biotechnology · AT

Funding

Austrian Science Fund FWF P 22249Austrian Science Fund FWF P 26946
6 · The paper itself

Abstract

When Escherichia coli encounters stress, the endoribonuclease MazF initiates a post-transcriptional response that results in the reprogramming of protein synthesis. By removing the 3΄-terminus of the 16S rRNA, MazF generates specialized ribosomes that selectively translate mRNAs likewise processed by MazF. Given the energy required for de novo ribosome biosynthesis, we considered the existence of a repair mechanism operating upon stress relief to recycle the modified ribosomes. Here, we show that the stress-ribosomes and the 3΄-terminal 16S rRNA fragment are stable during adverse conditions. Moreover, employing in vitro and in vivo approaches we demonstrate that the RNA ligase RtcB catalyzes the re-ligation of the truncated 16S rRNA present in specialized ribosomes Thereby their ability to translate canonical mRNAs is fully restored. Together, our findings not only provide a physiological function for the RNA ligase RtcB in bacteria but highlight the reversibility of ribosome heterogeneity, a crucial but hitherto undescribed concept for translational regulation.

Indexed as

Protein BiosynthesisAmino Acyl-tRNA SynthetasesDNA-Binding ProteinsEndoribonucleasesEscherichia coliEscherichia coli ProteinsGenetic HeterogeneityRibosomesRNA, Ribosomal, 16SAmino Acyl-tRNA SynthetasesDNA-Binding ProteinsEndoribonucleasesEscherichia coli ProteinsMazF protein, E coliRNA, Ribosomal, 16SRtcB protein, E coli

Identifiers

PMID27789694
PMCPMC5416887
OpenAlexW2545598638

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.