Evidence map›Paper›PMID 24975873›Full record

ArticleMolecular microbiology2014

Magnesium-dependent processes are targets of bacterial manganese toxicity.

Thomas H Hohle, Mark R O'Brian

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.9field-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

35 citing papers in PubMed, 53 citations in OpenAlex.

  1. Microbial metal physiology: ions to ecosystems.Nature reviews. Microbiology · 2025
    Review
  2. Review
  3. Article
  4. Disruption of zinc homeostasis reverses tigecycline resistance inFrontiers in cellular and infection microbiology · 2025
    Article
  5. The mntH gene of Burkholderia cenocepacia influences motility and quorum sensing to control virulence.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024
    Article
  6. Review
  7. Article
  8. TheJournal of bacteriology · 2024
    Article
  9. Article
  10. ThebioRxiv : the preprint server for biology · 2024
    Article
  11. Review
  12. Review
  13. Iron homeostasis inMicrobiology (Reading, England) · 2023
    Article
  14. Article
  15. Nramp: Deprive and conquer?Frontiers in cell and developmental biology · 2022
    Article
  16. Review
  17. Review
  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

2 authors at 2 institutions in 1 country.

Thomas H HohleDepartment of Biochemistry, State University of New York at Buffalo, Buffalo, NY, 14214, USA.
Mark R O'Brian
Buffalo State University · USUniversity at Buffalo, State University of New York · US

Funding

Regulation of bacterial manganese metabolismR01GM099667 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI O'BRIAN, MARK R · 2012 to 2016
$1.2M
NIGMS NIH HHS R01 GM099667PHS HHS R01 099667
6 · The paper itself

Abstract

A Bradyrhizobium japonicum mutant defective in the gene encoding the high-affinity Mn(2+) transporter MntH has a severe growth phenotype under manganese limitation. Here, we isolated suppressor mutants of an mntH strain that grew under manganese limitation, and activities of high-affinity Mn(2+) transport and Mn(2+) -dependent enzymes were partially rescued. The suppressor strains harbour gain-of-function mutations in the gene encoding the Mg(2+) channel MgtE. The MgtE variants likely allow Mn(2+) entry via loss of a gating mechanism that normally holds the transporter in the closed state when cellular Mg(2+) levels are high. Both MgtE-dependent and MgtE-independent suppressor phenotypes were recapitulated by magnesium-limited growth of the mntH strain. Growth studies of wild-type cells suggest that manganese is toxic to cells when environmental magnesium is low. Moreover, extracellular manganese and magnesium levels were manipulated to inhibit growth without substantially altering the intracellular content of either metal, implying that manganese toxicity depends on its cellular distribution rather than the absolute concentration. Mg(2+) -dependent enzyme activities were found to be inhibited or stimulated by Mn(2+) . We conclude that Mn(2+) can occupy Mg(2+) binding sites in cells, and suggest that Mg(2+) -dependent processes are targets of manganese toxicity.

Indexed as

AntiportersBacterial ProteinsBradyrhizobiumCation Transport ProteinsGene DeletionMagnesiumManganeseSuppression, GeneticAntiportersBacterial ProteinsCation Transport ProteinsMagnesiumManganeseMgtE protein, bacteriaMntH protein, bacteria

Identifiers

PMID24975873
PMCPMC4127137
OpenAlexW2124968651

What OpenQuestion holds

Textmetadata
LicenceTDM
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.