Evidence map›Paper›PMID 7928968›Full record

ArticleJournal of bacteriology1994

Purification of Rhizobium leguminosarum HypB, a nickel-binding protein required for hydrogenase synthesis.

L Rey, J Imperial, J M Palacios, T Ruiz-Argüeso

Open access · greenAbstract readComparative Study
In one paragraph

Article in Journal of bacteriology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
9.7field-weighted citation impact, top 2% 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

31 citing papers in PubMed, 96 citations in OpenAlex.

  1. Article
  2. Review
  3. Proteomic and Mutant Analysis of Hydrogenase Maturation Protein GeneInternational journal of molecular sciences · 2023
    Article
  4. A Comparative Study on Nickel Binding to Hpn-like Polypeptides from TwoInternational journal of molecular sciences · 2021
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Binding of Ni2+ to a histidine- and glutamine-rich protein, Hpn-like.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2008
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  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 1 institution in 1 country.

L ReyLaboratorio de Microbiología, Escuela Técnica Superior de Ingenieros Agrónomos, Universidad Politécnica de Madrid, Spain.
J Imperial
J M Palacios
T Ruiz-Argüeso
Universidad Politécnica de Madrid · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The products of the Rhizobium leguminosarum hyp gene cluster are necessary for synthesis of a functional uptake [NiFe] hydrogenase system in symbiosis with pea plants, and at least for HypB and HypF, a role in hydrogenase-specific nickel metabolism has been postulated (L. Rey, J. Murillo, Y. Hernando, E. Hidalgo, E. Cabrera, J. Imperial, and T. Ruiz-Argüeso, Mol. Microbiol. 8:471-481, 1993). The R. leguminosarum hypB gene product has been overexpressed in Escherichia coli and purified by immobilized nickel chelate affinity chromatography in a single step. The purified recombinant HypB protein was able to bind 3.9 +/- 0.1 Ni2+ ions per HypB monomer in solution. Co2+, Cu2+, and Zn2+ ions competed with Ni2+ with increasing efficiency. Monospecific HypB antibodies were raised and used to show that HypB is synthesized in R. leguminosarum microaerobic vegetative cells and pea bacteroids but not in R. leguminosarum aerobic cells. HypB protein synthesized by R. leguminosarum microaerobic vegetative cells could also be isolated by immobilized nickel chelate affinity chromatography. A histidine-rich region at the amino terminus of the protein (23-HGHHHH DGHHDHDHDHDHHRGDHEHDDHHH-54) is proposed to play a role in nickel binding, both in solution and in chelated form.

Indexed as

Bacterial ProteinsEscherichia coli ProteinsAerobiosisAmino AcidsAmino Acid SequenceAnaerobiosisCarrier ProteinsChelating AgentsChromatography, AffinityEscherichia coliGTP-Binding ProteinsHydrogenaseIsoelectric PointMolecular Sequence DataMolecular WeightNickelAmino AcidsBacterial ProteinsCarrier ProteinsChelating AgentsEscherichia coli ProteinsGTP-Binding ProteinsHydrogenaseHypB protein, bacteriaHypB protein, E coliNickelnickel-iron hydrogenaseNitrilotriacetic AcidNucleotidasesNucleotidesRecombinant Proteins

Identifiers

PMID7928968
PMCPMC196826
OpenAlexW1783635028

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.