Evidence map›Paper›PMID 32723821›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Progression from remodeling to hibernation of ribosomes in zinc-starved mycobacteria.

Yunlong Li, Jamie H Corro, Christopher D Palmer, Anil K Ojha

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

27 citing papers in PubMed, 28 citations in OpenAlex.

  1. Ribosome hibernation in zinc-starvedMicrobiology spectrum · 2026
    Article
  2. Article
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  4. Review
  5. iScience · 2026
    Article
  6. Journal of bacteriology · 2026
    Review
  7. Article
  8. Article
  9. Article
  10. AACS infectious diseases · 2025
    Article
  11. Article
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  14. Article
  15. Review
  16. Starvation sensing by mycobacterial RelA/SpoT homologue through constitutive surveillance of translation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Article
  18. Review
  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

4 authors at 1 institution in 1 country.

Yunlong LiDivision of Genetics, Wadsworth Center, New York State Department of Health, Albany, NY 12208.
Jamie H CorroDivision of Genetics, Wadsworth Center, New York State Department of Health, Albany, NY 12208.
Christopher D PalmerLaboratory of Inorganic and Nuclear Chemistry, Wadsworth Center, New York State Department of Health, Albany, NY 12202.
Anil K OjhaDivision of Genetics, Wadsworth Center, New York State Department of Health, Albany, NY 12208; anil.ojha@health.ny.gov.ORCID 0000-0001-5940-2643
New York State Department of Health · US

Funding

Alternative Ribosomes & Antibiotic Tolerance in MycobacteriaR01AI132422 · NIAID · WADSWORTH CENTER · PI RAJENDRA K AGRAWAL, Anil Kumar Ojha · 2017 to 2026
$3.8M
Physiology of Mycobacterium Tuberculosis with Hibernating RibosomesR21AI144474 · NIAID · WADSWORTH CENTER · PI OJHA, ANIL KUMAR · 2019 to 2020
$466k
NIAID NIH HHS R01 AI132422NIAID NIH HHS R21 AI144474
6 · The paper itself

Abstract

Zinc starvation in mycobacteria leads to remodeling of ribosomes, in which multiple ribosomal (r-) proteins containing the zinc-binding CXXC motif are replaced by their motif-free paralogues, collectively called C- r-proteins. We previously reported that the 70S C- ribosome is exclusively targeted for hibernation by mycobacterial-specific protein Y (Mpy), which binds to the decoding center and stabilizes the ribosome in an inactive and drug-resistant state. In this study, we delineate the conditions for ribosome remodeling and hibernation and provide further insight into how zinc depletion induces Mpy recruitment to C- ribosomes. Specifically, we show that ribosome hibernation in a batch culture is induced at an approximately two-fold lower cellular zinc concentration than remodeling. We further identify a growth phase in which the C- ribosome remains active, while its hibernation is inhibited by the caseinolytic protease (Clp) system in a zinc-dependent manner. The Clp protease system destabilizes a zinc-bound form of Mpy recruitment factor (Mrf), which is stabilized upon further depletion of zinc, presumably in a zinc-free form. Stabilized Mrf binds to the 30S subunit and recruits Mpy to the ribosome. Replenishment of zinc to cells harboring hibernating ribosomes restores Mrf instability and dissociates Mpy from the ribosome. Finally, we demonstrate zinc-responsive binding of Mpy to ribosomes in

Indexed as

AnimalsAntibiotics, AntitubercularBacterial ProteinsDrug ToleranceEndopeptidase ClpMiceMycobacterium tuberculosisProtein Processing, Post-TranslationalRibosomal ProteinsRibosomesRibosome SubunitsZincAntibiotics, AntitubercularBacterial ProteinsEndopeptidase ClpRibosomal ProteinsZincClp proteasedrug tolerancepersistenceribosome hibernationtuberculosis

Identifiers

PMID32723821
PMCPMC7431043
OpenAlexW3045835921

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.