Evidence map›Paper›PMID 24794564›Full record

ArticleJournal of bacteriology2014

Novel MntR-independent mechanism of manganese homeostasis in Escherichia coli by the ribosome-associated protein HflX.

Gursharan Kaur, Sandeepan Sengupta, Vineet Kumar, Aruna Kumari, Aditi Ghosh, Pradeep Parrack, Dipak Dutta

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

22 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
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  3. Proteomic profiling of zinc homeostasis mechanisms inbioRxiv : the preprint server for biology · 2025
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  7. Manganese transporters regulate the resumption of replication in hydrogen peroxide-stressed Escherichia coli.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. HflX protein protectsJournal of biosciences · 2018
    Article
  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

7 authors at 2 institutions in 1 country.

Gursharan KaurLaboratory of Molecular Biochemistry, CSIR-Institute of Microbial Technology, Chandigarh, India.
Sandeepan SenguptaDepartment of Biochemistry, Bose Institute, Kolkata, India.
Vineet KumarLaboratory of Molecular Biochemistry, CSIR-Institute of Microbial Technology, Chandigarh, India.
Aruna KumariLaboratory of Molecular Biochemistry, CSIR-Institute of Microbial Technology, Chandigarh, India.
Aditi GhoshDepartment of Biochemistry, Bose Institute, Kolkata, India.
Pradeep ParrackDepartment of Biochemistry, Bose Institute, Kolkata, India.
Dipak DuttaLaboratory of Molecular Biochemistry, CSIR-Institute of Microbial Technology, Chandigarh, India dutta@imtech.res.in.
Institute of Microbial Technology · INBose Institute · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Manganese is a micronutrient required for activities of several important enzymes under conditions of oxidative stress and iron starvation. In Escherichia coli, the manganese homeostasis network primarily constitutes a manganese importer (MntH) and an exporter (MntP), which are regulated by the MntR dual regulator. In this study, we find that deletion of E. coli hflX, which encodes a ribosome-associated GTPase with unknown function, renders extreme manganese sensitivity characterized by arrested cell growth, filamentation, lower rate of replication, and DNA damage. We demonstrate that perturbation by manganese induces unprecedented influx of manganese in ΔhflX cells compared to that in the wild-type E. coli strain. Interestingly, our study indicates that the imbalance in manganese homeostasis in the ΔhflX strain is independent of the MntR regulon. Moreover, the influx of manganese leads to a simultaneous influx of zinc and inhibition of iron import in ΔhflX cells. In order to review a possible link of HflX with the λ phage life cycle, we performed a lysis-lysogeny assay to show that the Mn-perturbed ΔhflX strain reduces the frequency of lysogenization of the phage. This observation raises the possibility that the induced zinc influx in the manganese-perturbed ΔhflX strain stimulates the activity of the zinc-metalloprotease HflB, the key determinant of the lysis-lysogeny switch. Finally, we propose that manganese-mediated autophosphorylation of HflX plays a central role in manganese, zinc, and iron homeostasis in E. coli cells.

Indexed as

Biological TransportEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialGTP-Binding ProteinsHomeostasisManganeseRepressor ProteinsSignal TransductionEscherichia coli ProteinsGTP-Binding ProteinsHflX protein, E coliManganeseMntR protein, E coliRepressor Proteins

Identifiers

PMID24794564
PMCPMC4097593
OpenAlexW2061842825

What OpenQuestion holds

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Read underepoch 390

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.