Evidence map›Paper›PMID 20851900›Full record

ArticleJournal of bacteriology2010

A Rhodobacter capsulatus member of a universal permease family imports molybdate and other oxyanions.

Jonathan Gisin, Alexandra Müller, Yvonne Pfänder, Silke Leimkühler, Franz Narberhaus, Bernd Masepohl

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

23 citing papers in PubMed, 40 citations in OpenAlex.

  1. Association of ABCG5 and ABCG8 Transporters with Sitosterolemia.Advances in experimental medicine and biology · 2024
    Review
  2. [Construction and biological characterization of aNan fang yi ke da xue xue bao = Journal of Southern Medical University · 2023
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

6 authors at 3 institutions in 1 country.

Jonathan GisinRuhr-Universität Bochum, Fakultät für Biologie und Biotechnologie, Biologie der Mikroorganismen, Bochum, Germany.
Alexandra Müller
Yvonne Pfänder
Silke Leimkühler
Franz Narberhaus
Bernd Masepohl
Ruhr University Bochum · DEUniversity of Konstanz · DEUniversity of Potsdam · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Molybdenum (Mo) is an important trace element that is toxic at high concentrations. To resolve the mechanisms underlying Mo toxicity, Rhodobacter capsulatus mutants tolerant to high Mo concentrations were isolated by random transposon Tn5 mutagenesis. The insertion sites of six independent isolates mapped within the same gene predicted to code for a permease of unknown function located in the cytoplasmic membrane. During growth under Mo-replete conditions, the wild-type strain accumulated considerably more Mo than the permease mutant. For mutants defective for the permease, the high-affinity molybdate importer ModABC, or both transporters, in vivo Mo-dependent nitrogenase (Mo-nitrogenase) activities at different Mo concentrations suggested that ModABC and the permease import molybdate in nanomolar and micromolar ranges, respectively. Like the permease mutants, a mutant defective for ATP sulfurylase tolerated high Mo concentrations, suggesting that ATP sulfurylase is the main target of Mo inhibition in R. capsulatus. Sulfate-dependent growth of a double mutant defective for the permease and the high-affinity sulfate importer CysTWA was reduced compared to those of the single mutants, implying that the permease plays an important role in sulfate uptake. In addition, permease mutants tolerated higher tungstate and vanadate concentrations than the wild type, suggesting that the permease acts as a general oxyanion importer. We propose to call this permease PerO (for oxyanion permease). It is the first reported bacterial molybdate transporter outside the ABC transporter family.

Indexed as

AnionsBacterial ProteinsDNA, BacterialDNA Transposable ElementsDrug Resistance, BacterialMembrane Transport ProteinsMolecular Sequence DataMolybdenumMutagenesis, InsertionalRhodobacter capsulatusSequence Analysis, DNASulfate AdenylyltransferaseTungsten CompoundsVanadatesAnionsBacterial ProteinsDNA, BacterialDNA Transposable ElementsMembrane Transport ProteinsmolybdateMolybdenumSulfate AdenylyltransferasetungstateTungsten CompoundsVanadates

Identifiers

PMID20851900
PMCPMC2976454
OpenAlexW2113029709

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.