Evidence map›Paper›PMID 26981620›Full record

ArticlePLoS biology2016

MamO Is a Repurposed Serine Protease that Promotes Magnetite Biomineralization through Direct Transition Metal Binding in Magnetotactic Bacteria.

David M Hershey, Xuefeng Ren, Ryan A Melnyk, Patrick J Browne, Ertan Ozyamak, Stephanie R Jones, Michelle C Y Chang, James H Hurley, Arash Komeili

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2016. 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
4.0field-weighted citation impact, top 6% 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, 49 citations in OpenAlex.

  1. Review
  2. Magnetochrome-catalyzed oxidation of ferrous iron by MamP enables magnetite crystal growth in the magnetotactic bacterium AMB-1.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. The Mantle Transcriptome ofAnimals : an open access journal from MDPI · 2022
    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. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Magnetosome biogenesis in magnetotactic bacteria.Nature reviews. Microbiology · 2016
    Review
  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

9 authors at 2 institutions in 1 country.

David M HersheyDepartment of Plant and Microbial Biology, University of California, Berkeley, California, United States of America.
Xuefeng RenDepartment of Molecular and Cellular Biology, University of California, Berkeley, California, United States of America.
Ryan A MelnykPhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California, United States of America.
Patrick J BrowneDepartment of Plant and Microbial Biology, University of California, Berkeley, California, United States of America.
Ertan OzyamakDepartment of Plant and Microbial Biology, University of California, Berkeley, California, United States of America.
Stephanie R JonesDepartment of Chemistry, University of California, Berkeley, California, United States of America.
Michelle C Y ChangDepartment of Molecular and Cellular Biology, University of California, Berkeley, California, United States of America.
James H HurleyDepartment of Molecular and Cellular Biology, University of California, Berkeley, California, United States of America.
Arash KomeiliDepartment of Plant and Microbial Biology, University of California, Berkeley, California, United States of America.
University of California, Berkeley · USLawrence Berkeley National Laboratory · US

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

Many living organisms transform inorganic atoms into highly ordered crystalline materials. An elegant example of such biomineralization processes is the production of nano-scale magnetic crystals in magnetotactic bacteria. Previous studies implicated the involvement of two putative serine proteases, MamE and MamO, during the early stages of magnetite formation in Magnetospirillum magneticum AMB-1. Here, using genetic analysis and X-ray crystallography, we show that MamO has a degenerate active site, rendering it incapable of protease activity. Instead, MamO promotes magnetosome formation through two genetically distinct, noncatalytic activities: activation of MamE-dependent proteolysis of biomineralization factors and direct binding to transition metal ions. By solving the structure of the protease domain bound to a metal ion, we identify a surface-exposed di-histidine motif in MamO that contributes to metal binding and show that it is required to initiate biomineralization in vivo. Finally, we find that pseudoproteases are widespread in magnetotactic bacteria and that they have evolved independently in three separate taxa. Our results highlight the versatility of protein scaffolds in accommodating new biochemical activities and provide unprecedented insight into the earliest stages of biomineralization.

Indexed as

Evolution, MolecularBacterial ProteinsCatalytic DomainFerrosoferric OxideMagnetospirillumProteolysisSerine ProteasesTransition ElementsBacterial ProteinsFerrosoferric OxideSerine ProteasesTransition Elements

Identifiers

PMID26981620
PMCPMC4794232
OpenAlexW2300071189

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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.