Evidence map›Paper›PMID 20639861›Full record

ArticleNature2010

Microbial metalloproteomes are largely uncharacterized.

Aleksandar Cvetkovic, Angeli Lal Menon, Michael P Thorgersen, Joseph W Scott, Farris L Poole, Francis E Jenney, W Andrew Lancaster, Jeremy L Praissman, Saratchandra Shanmukh, Brian J Vaccaro and 7 more

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In one paragraph

Article in Nature, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 159 papers.

0numbers the graph read from it
0cells of the map it votes in
159citing papers in PubMed
24.3field-weighted citation impact, top 1% 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

159 citing papers in PubMed, 358 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Microbial metal physiology: ions to ecosystems.Nature reviews. Microbiology · 2025
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Proteomic strategies to interrogate the Fe-S proteome.Biochimica et biophysica acta. Molecular cell research · 2024
    Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. 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
  19. Article
  20. Review

99 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

17 authors at 3 institutions in 1 country.

Aleksandar CvetkovicDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602, USA.
Angeli Lal Menon
Michael P Thorgersen
Joseph W Scott
Farris L Poole
Francis E Jenney
W Andrew Lancaster
Jeremy L Praissman
Saratchandra Shanmukh
Brian J Vaccaro
Sunia A Trauger
Ewa Kalisiak
Junefredo V Apon
Gary Siuzdak
Steven M Yannone
John A Tainer
Michael W W Adams
University of Georgia · USScripps Research Institute · USLawrence Berkeley National Laboratory · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Metal ion cofactors afford proteins virtually unlimited catalytic potential, enable electron transfer reactions and have a great impact on protein stability. Consequently, metalloproteins have key roles in most biological processes, including respiration (iron and copper), photosynthesis (manganese) and drug metabolism (iron). Yet, predicting from genome sequence the numbers and types of metal an organism assimilates from its environment or uses in its metalloproteome is currently impossible because metal coordination sites are diverse and poorly recognized. We present here a robust, metal-based approach to determine all metals an organism assimilates and identify its metalloproteins on a genome-wide scale. This shifts the focus from classical protein-based purification to metal-based identification and purification by liquid chromatography, high-throughput tandem mass spectrometry (HT-MS/MS) and inductively coupled plasma mass spectrometry (ICP-MS) to characterize cytoplasmic metalloproteins from an exemplary microorganism (Pyrococcus furiosus). Of 343 metal peaks in chromatography fractions, 158 did not match any predicted metalloprotein. Unassigned peaks included metals known to be used (cobalt, iron, nickel, tungsten and zinc; 83 peaks) plus metals the organism was not thought to assimilate (lead, manganese, molybdenum, uranium and vanadium; 75 peaks). Purification of eight of 158 unexpected metal peaks yielded four novel nickel- and molybdenum-containing proteins, whereas four purified proteins contained sub-stoichiometric amounts of misincorporated lead and uranium. Analyses of two additional microorganisms (Escherichia coli and Sulfolobus solfataricus) revealed species-specific assimilation of yet more unexpected metals. Metalloproteomes are therefore much more extensive and diverse than previously recognized, and promise to provide key insights for cell biology, microbial growth and toxicity mechanisms.

Indexed as

Bacterial ProteinsChromatography, LiquidEscherichia coliMetalloproteinsMetalsProteomeProteomicsPyrococcus furiosusSulfolobus solfataricusTandem Mass SpectrometryBacterial ProteinsMetalloproteinsMetalsProteome

Identifiers

PMID20639861
OpenAlexW1999491456

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.