Evidence map›Paper›PMID 24782310›Full record

ArticleThe Journal of biological chemistry2014

A bacterial iron exporter for maintenance of iron homeostasis.

Siva Sankari, Mark R O'Brian

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

21 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Bacterial iron detoxification at the molecular level.The Journal of biological chemistry · 2020
    Review
  9. Article
  10. Iron Acquisition by Bacterial Pathogens: Beyond Tris-Catecholate Complexes.Chembiochem : a European journal of chemical biology · 2020
    Review
  11. Article
  12. Review
  13. Article
  14. Ferrous iron efflux systems in bacteria.Metallomics : integrated biometal science · 2017
    Review
  15. Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.Microbiology and molecular biology reviews : MMBR · 2017
    Review
  16. Article
  17. 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

2 authors at 1 institution in 1 country.

Siva SankariFrom the Department of Biochemistry, State University of New York at Buffalo, Buffalo, New York 14214.
Mark R O'BrianFrom the Department of Biochemistry, State University of New York at Buffalo, Buffalo, New York 14214 mrobrian@buffalo.edu.
University 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

Nutritional iron acquisition by bacteria is well described, but almost nothing is known about bacterial iron export even though it is likely to be an important homeostatic mechanism. Here, we show that Bradyrhizobium japonicum MbfA (Blr7895) is an inner membrane protein expressed in cells specifically under high iron conditions. MbfA contains an N-terminal ferritin-like domain (FLD) and a C-terminal domain homologous to the eukaryotic vacuolar membrane Fe(2+)/Mn(2+) transporter CCC1. An mbfA deletion mutant is severely defective in iron export activity, contains >2-fold more intracellular iron than the parent strain, and displays an aberrant iron-dependent gene expression phenotype. B. japonicum is highly resistant to iron and H2O2 stresses, and MbfA contributes substantially to this as determined by phenotypes of the mbfA mutant strain. The N-terminal FLD was localized to the cytoplasmic side of the inner membrane. Substitution mutations in the putative iron-binding amino acid residues E20A and E107A within the N-terminal FLD abrogate iron export activity and stress response function. Purified soluble FLD oxidizes ferrous iron (Fe(2+)) to incorporate ferric iron (Fe(3+)) in a 2:1 iron:protein ratio, which does not occur in the E20A/E107A mutant. The FLD fragment is a dimer in solution, implying that the MbfA exporter functions as a dimer. MbfA belongs to a protein family found in numerous prokaryotic genera. The findings strongly suggest that iron export plays an important role in bacterial iron homeostasis.

Indexed as

HomeostasisBradyrhizobiumIronMutationPolymerase Chain ReactionIronBacterial MetabolismIron MetabolismMembrane TransportMetal HomeostasisOxidative Stress

Identifiers

PMID24782310
PMCPMC4047416
OpenAlexW2029012493

What OpenQuestion holds

Textmetadata
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.