Evidence map›Paper›PMID 17911085›Full record

ArticleMolecular & cellular proteomics : MCP2007

Periplasmic proteins of the extremophile Acidithiobacillus ferrooxidans: a high throughput proteomics analysis.

An Chi, Lissette Valenzuela, Simon Beard, Aaron J Mackey, Jeffrey Shabanowitz, Donald F Hunt, Carlos A Jerez

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.8field-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

34 citing papers in PubMed, 97 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Penicillin-binding protein redundancy inApplied and environmental microbiology · 2024
    Article
  5. Article
  6. Article
  7. Article
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  10. Review
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  12. Review
  13. Article
  14. Article
  15. Article
  16. Deciphering the Role of Multiple Thioredoxin Fold Proteins ofInternational journal of molecular sciences · 2020
    Article
  17. Insights into the Periplasmic Proteins ofInternational journal of molecular sciences · 2019
    Article
  18. Iron and sulfur oxidation pathways of Acidithiobacillus ferrooxidans.World journal of microbiology & biotechnology · 2019
    Review
  19. Article
  20. Acidithiobacillus ferrooxidans and its potential application.Extremophiles : life under extreme conditions · 2018
    Review
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

7 authors at 2 institutions in 2 countries.

An ChiDepartment of Biology and Cell Dynamics and Biotechnology Institute, Faculty of Sciences, University of Chile, Santiago 7800024, Chile.
Lissette Valenzuela
Simon Beard
Aaron J Mackey
Jeffrey Shabanowitz
Donald F Hunt
Carlos A Jerez
University of Virginia · USUniversity of Chile · CL

Funding

PROTEIN SEQUENCING BY TANDEM MASS SPECTROMETRYR01GM037537 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI HUNT, DONALD F · 1987 to 2023
$17.8M
NIGMS NIH HHS R01 GM037537
6 · The paper itself

Abstract

Acidithiobacillus ferrooxidans is a chemolithoautotrophic acidophile capable of obtaining energy by oxidizing ferrous iron or sulfur compounds such as metal sulfides. Some of the proteins involved in these oxidations have been described as forming part of the periplasm of this extremophile. The detailed study of the periplasmic components constitutes an important area to understand the physiology and environmental interactions of microorganisms. Proteomics analysis of the periplasmic fraction of A. ferrooxidans ATCC 23270 was performed by using high resolution linear ion trap-FT MS. We identified a total of 131 proteins in the periplasm of the microorganism grown in thiosulfate. When possible, functional categories were assigned to the proteins: 13.8% were transport and binding proteins, 14.6% were several kinds of cell envelope proteins, 10.8% were involved in energy metabolism, 10% were related to protein fate and folding, 10% were proteins with unknown functions, and 26.1% were proteins without homologues in databases. These last proteins are most likely characteristic of A. ferrooxidans and may have important roles yet to be assigned. The majority of the periplasmic proteins from A. ferrooxidans were very basic compared with those of neutrophilic microorganisms such as Escherichia coli, suggesting a special adaptation of the chemolithoautotrophic bacterium to its very acidic environment. The high throughput proteomics approach used here not only helps to understand the physiology of this extreme acidophile but also offers an important contribution to the functional annotation for the available genomes of biomining microorganisms such as A. ferrooxidans for which no efficient genetic systems are available to disrupt genes by procedures such as homologous recombination.

Indexed as

ProteomicsAcidithiobacillusBacterial ProteinsChromatography, LiquidMass SpectrometryPeriplasmBacterial Proteins

Identifiers

PMID17911085
PMCPMC4631397
OpenAlexW2129168664

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.