Evidence map›Paper›PMID 17965152›Full record

ArticleJournal of bacteriology2008

The major magnetosome proteins MamGFDC are not essential for magnetite biomineralization in Magnetospirillum gryphiswaldense but regulate the size of magnetosome crystals.

André Scheffel, Astrid Gärdes, Karen Grünberg, Gerhard Wanner, Dirk Schüler

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

83 citing papers in PubMed, 191 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Engineering Magnetotactic Bacteria as Medical Microrobots.Advanced materials (Deerfield Beach, Fla.) · 2025
    Review
  5. Article
  6. Bacterial Organelles in Iron Physiology.Molecular microbiology · 2024
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. A Magnetosome-Based Platform for Flow Biocatalysis.ACS applied materials & interfaces · 2022
    Article
  15. A protease-mediated switch regulates the growth of magnetosome organelles inProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

23 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

André ScheffelMax Planck Institute for Marine Microbiology, Celsiusstr. 1, D-28359 Bremen, Germany.
Astrid Gärdes
Karen Grünberg
Gerhard Wanner
Dirk Schüler
Max Planck Institute for Marine Microbiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Magnetospirillum gryphiswaldense and related magnetotactic bacteria form magnetosomes, which are membrane-enclosed organelles containing crystals of magnetite (Fe3O4) that cause the cells to orient in magnetic fields. The characteristic sizes, morphologies, and patterns of alignment of magnetite crystals are controlled by vesicles formed of the magnetosome membrane (MM), which contains a number of specific proteins whose precise roles in magnetosome formation have remained largely elusive. Here, we report on a functional analysis of the small hydrophobic MamGFDC proteins, which altogether account for nearly 35% of all proteins associated with the MM. Although their high levels of abundance and conservation among magnetotactic bacteria had suggested a major role in magnetosome formation, we found that the MamGFDC proteins are not essential for biomineralization, as the deletion of neither mamC, encoding the most abundant magnetosome protein, nor the entire mamGFDC operon abolished the formation of magnetite crystals. However, cells lacking mamGFDC produced crystals that were only 75% of the wild-type size and were less regular than wild-type crystals with respect to morphology and chain-like organization. The inhibition of crystal formation could not be eliminated by increased iron concentrations. The growth of mutant crystals apparently was not spatially constrained by the sizes of MM vesicles, as cells lacking mamGFDC formed vesicles with sizes and shapes nearly identical to those formed by wild-type cells. However, the formation of wild-type-size magnetite crystals could be gradually restored by in-trans complementation with one, two, and three genes of the mamGFDC operon, regardless of the combination, whereas the expression of all four genes resulted in crystals exceeding the wild-type size. Our data suggest that the MamGFDC proteins have partially redundant functions and, in a cumulative manner, control the growth of magnetite crystals by an as-yet-unknown mechanism.

Indexed as

MagneticsBacterial ProteinsBiotransformationCulture MediaDNA, BacterialFerrosoferric OxideGenetic Complementation TestMagnetospirillumMutagenesisOrganellesPlasmidsBacterial ProteinsCulture MediaDNA, BacterialFerrosoferric Oxide

Identifiers

PMID17965152
PMCPMC2223754
OpenAlexW1978870027

What OpenQuestion holds

Textmetadata
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.