Evidence map›Paper›PMID 22016389›Full record

ArticleThe Journal of biological chemistry2011

Protein interactions and localization of the Escherichia coli accessory protein HypA during nickel insertion to [NiFe] hydrogenase.

Kim C Chan Chung, Deborah B Zamble

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.8field-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

24 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Bimodal Nickel-Binding Site onInorganic chemistry · 2019
    Article
  8. Article
  9. Article
  10. Crystal structures of a [NiFe] hydrogenase large subunit HyhL in an immature state in complex with a Ni chaperone HypA.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  11. Co(II) and Ni(II) binding of theThe Journal of biological chemistry · 2018
    Article
  12. Functional disruption of peroxiredoxin by bismuth antiulcer drugs attenuates Helicobacter pylori survival.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017
    Article
  13. Article
  14. Review
  15. Review
  16. Biosynthesis of Salmonella enterica [NiFe]-hydrogenase-5: probing the roles of system-specific accessory proteins.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016
    Article
  17. Review
  18. Structural basis of a Ni acquisition cycle for [NiFe] hydrogenase by Ni-metallochaperone HypA and its enhancer.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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

2 authors at 1 institution in 1 country.

Kim C Chan ChungDepartment of Chemistry, University of Toronto, Toronto, Ontario M5S 3H6, Canada.
Deborah B Zamble
University of Toronto · CA

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Nickel delivery during maturation of Escherichia coli [NiFe] hydrogenase 3 includes the accessory proteins HypA, HypB, and SlyD. Although the isolated proteins have been characterized, little is known about how they interact with each other and the hydrogenase 3 large subunit, HycE. In this study the complexes of HypA and HycE were investigated after modification with the Strep-tag II. Multiprotein complexes containing HypA, HypB, SlyD, and HycE were observed, consistent with the assembly of a single nickel insertion cluster. An interaction between HypA and HycE did not require the other nickel insertion proteins, but HypB was not found with the large subunit in the absence of HypA. The HypA-HycE complex was not detected in the absence of the HypC or HypD proteins, involved in the preceding iron insertion step, and this interaction is enhanced by nickel brought into the cell by the NikABCDE membrane transporter. Furthermore, without the hydrogenase 1, 2, and 3 large subunits, complexes between HypA, HypB, and SlyD were observed. These results support the hypothesis that HypA acts as a scaffold for assembly of the nickel insertion proteins with the hydrogenase precursor protein after delivery of the iron center. At different stages of the hydrogenase maturation process, HypA was observed at or near the cell membrane by using fluorescence confocal microscopy, as was HycE, suggesting membrane localization of the nickel insertion event.

Indexed as

Blotting, WesternCarrier ProteinsElectrophoresis, Polyacrylamide GelEscherichia coli ProteinsGTP-Binding ProteinsHydrogenaseIntracellular Signaling Peptides and ProteinsMicroscopy, FluorescenceNickelPeptidylprolyl IsomeraseProtein BindingTandem Mass SpectrometryCarrier ProteinsEscherichia coli ProteinsGTP-Binding ProteinshycE protein, E coliHydrogenaseHypA protein, E coliHypB protein, E coliIntracellular Signaling Peptides and ProteinsNickelnickel-iron hydrogenasePeptidylprolyl IsomeraseSlyD protein, E coli

Identifiers

PMID22016389
PMCPMC3234881
OpenAlexW1969557555

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.