Evidence map›Paper›PMID 33125369›Full record

ArticlePLoS biology2020

Differences in structure and hibernation mechanism highlight diversification of the microsporidian ribosome.

Kai Ehrenbolger, Nathan Jespersen, Himanshu Sharma, Yuliya Y Sokolova, Yuri S Tokarev, Charles R Vossbrinck, Jonas Barandun

Abstract read
In one paragraph

Article in PLoS biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Hibernating ribosomes as drug targets?Frontiers in microbiology · 2024
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Comparative Genomics of Microsporidia.Experientia supplementum (2012) · 2022
    Article
  14. Impact of Genome Reduction in Microsporidia.Experientia supplementum (2012) · 2022
    Article
  15. 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

7 authors.

Kai EhrenbolgerDepartment of Molecular Biology, Laboratory for Molecular Infection Medicine Sweden, Umeå Centre for Microbial Research, Science for Life Laboratory, Umeå University, Umeå, Sweden.ORCID 0000-0003-1312-5825
Nathan JespersenDepartment of Molecular Biology, Laboratory for Molecular Infection Medicine Sweden, Umeå Centre for Microbial Research, Science for Life Laboratory, Umeå University, Umeå, Sweden.ORCID 0000-0001-6931-1526
Himanshu SharmaDepartment of Molecular Biology, Laboratory for Molecular Infection Medicine Sweden, Umeå Centre for Microbial Research, Science for Life Laboratory, Umeå University, Umeå, Sweden.
Yuliya Y SokolovaDepartment of Microbiology, Immunology, and Tropical Medicine, School of Medicine and Health Sciences, George Washington University, Washington, District of Columbia, United States of America.ORCID 0000-0003-0448-7226
Yuri S TokarevAll-Russian Institute of Plant Protection, St. Petersburg, Russia.ORCID 0000-0003-0524-0778
Charles R VossbrinckDepartment of Environmental Science, Connecticut Agricultural Experiment Station, New Haven, Connecticut, United States of America.
Jonas BarandunDepartment of Molecular Biology, Laboratory for Molecular Infection Medicine Sweden, Umeå Centre for Microbial Research, Science for Life Laboratory, Umeå University, Umeå, Sweden.ORCID 0000-0003-2971-8190

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Assembling and powering ribosomes are energy-intensive processes requiring fine-tuned cellular control mechanisms. In organisms operating under strict nutrient limitations, such as pathogenic microsporidia, conservation of energy via ribosomal hibernation and recycling is critical. The mechanisms by which hibernation is achieved in microsporidia, however, remain poorly understood. Here, we present the cryo-electron microscopy structure of the ribosome from Paranosema locustae spores, bound by the conserved eukaryotic hibernation and recycling factor Lso2. The microsporidian Lso2 homolog adopts a V-shaped conformation to bridge the mRNA decoding site and the large subunit tRNA binding sites, providing a reversible ribosome inactivation mechanism. Although microsporidian ribosomes are highly compacted, the P. locustae ribosome retains several rRNA segments absent in other microsporidia, and represents an intermediate state of rRNA reduction. In one case, the near complete reduction of an expansion segment has resulted in a single bound nucleotide, which may act as an architectural co-factor to stabilize a protein-protein interface. The presented structure highlights the reductive evolution in these emerging pathogens and sheds light on a conserved mechanism for eukaryotic ribosome hibernation.

Indexed as

Cryoelectron MicroscopyEvolution, MolecularFungal ProteinsMicrosporidiaModels, MolecularNucleotidesProtein BindingRibosomal ProteinsRibosomesFungal ProteinsNucleotidesRibosomal Proteins

Identifiers

PMID33125369
PMCPMC7644102

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Registered trials

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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.