Evidence map›Paper›PMID 21414040›Full record

ArticleMolecular microbiology2011

The HtrA/DegP family protease MamE is a bifunctional protein with roles in magnetosome protein localization and magnetite biomineralization.

Anna Quinlan, Dorothée Murat, Hojatollah Vali, Arash Komeili

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

42 citing papers in PubMed, 93 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Periplasmic Bacterial Biomineralization of Copper Sulfide Nanoparticles.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Article
  7. Article
  8. Article
  9. 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
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Magnetosome biogenesis in magnetotactic bacteria.Nature reviews. Microbiology · 2016
    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 2 institutions in 2 countries.

Anna QuinlanDepartment of Molecular and Cell Biology, University of California Berkeley, 111 Koshland Hall, Berkeley, CA 94720, USA.
Dorothée Murat
Hojatollah Vali
Arash Komeili
University of California, Berkeley · USMcGill University · CA

Funding

Molecular Mechanisms of Organelle Assembly by the Prokaryotic Actin Homolog MamKR01GM084122 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KOMEILI, ARASH · 2009 to 2017
$2.8M
NIGMS NIH HHS R01 GM084122NIGMS NIH HHS R01GM084122
6 · The paper itself

Abstract

Magnetotactic bacteria contain nanometre-sized, membrane-bound organelles, called magnetosomes, which are tasked with the biomineralization of small crystals of the iron oxide magnetite allowing the organism to use geomagnetic field lines for navigation. A key player in this process is the HtrA/DegP family protease MamE. In its absence, Magnetospirillum magneticum str AMB-1 is able to form magnetosome membranes but not magnetite crystals, a defect previously linked to the mislocalization of magnetosome proteins. In this work we use a directed genetic approach to find that MamE, and another predicted magnetosome-associated protease, MamO, likely function as proteases in vivo. However, as opposed to the complete loss of mamE where no biomineralization is observed, the protease-deficient variant of this protein still supports the initiation and formation of small, 20 nm-sized crystals of magnetite, too small to hold a permanent magnetic dipole moment. This analysis also reveals that MamE is a bifunctional protein with a protease-independent role in magnetosome protein localization and a protease-dependent role in maturation of small magnetite crystals. Together, these results imply the existence of a previously unrecognized 'checkpoint' in biomineralization where MamE moderates the completion of magnetite formation and thus committal to magneto-aerotaxis as the organism's dominant mode of navigating the environment.

Indexed as

Amino Acid SequenceBacterial ProteinsFerrosoferric OxideGenes, BacterialHeat-Shock ProteinsMagneticsMagnetosomesMagnetospirillumMembrane ProteinsMicroscopy, FluorescenceMutagenesis, Site-DirectedPeptide HydrolasesPeriplasmic ProteinsSequence AlignmentSerine EndopeptidasesBacterial ProteinsDegP proteaseFerrosoferric OxideHeat-Shock ProteinsMembrane ProteinsPeptide HydrolasesPeriplasmic ProteinsSerine Endopeptidases

Identifiers

PMID21414040
PMCPMC3091955
OpenAlexW2115900881

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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.