Evidence map›Paper›PMID 30353723›Full record

ArticleBiochemistry2019

Two ABC Transporters and a Periplasmic Metallochaperone Participate in Zinc Acquisition in Paracoccus denitrificans.

Durga P Neupane, Santosh Kumar, Erik T Yukl

Open access · bronzeAbstract read
In one paragraph

Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

16 citing papers in PubMed, 20 citations in OpenAlex.

  1. Deep learning-drivenSynthetic and systems biotechnology · 2027
    Article
  2. Article
  3. A periplasmic zinc capture protein enhances the resistance ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Two zinc ABC transporters contribute toFrontiers in plant science · 2025
    Article
  5. Article
  6. Exposure ofJournal of fungi (Basel, Switzerland) · 2023
    Article
  7. Zinc acquisition and its contribution toFrontiers in cellular and infection microbiology · 2023
    Article
  8. Structure and Function of the Zinc Binding Protein ZrgA fromInternational journal of molecular sciences · 2022
    Article
  9. Conformational flexibility in the zinc solute-binding protein ZnuA.Acta crystallographica. Section F, Structural biology communications · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
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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

3 authors at 2 institutions in 1 country.

Durga P NeupaneDepartment of Chemistry and Biochemistry , New Mexico State University , Las Cruces , New Mexico 88003 , United States.
Santosh KumarDepartment of Biological Sciences , University of Texas at Dallas , Richardson , Texas 75080 , United States.
Erik T YuklDepartment of Chemistry and Biochemistry , New Mexico State University , Las Cruces , New Mexico 88003 , United States.ORCID 0000-0001-6519-6938
New Mexico State University · USThe University of Texas at Dallas · US

Funding

Periplasmic Zinc Management and Homeostasis in Paracoccus denitrificansR01GM122819 · NIGMS · NEW MEXICO STATE UNIVERSITY LAS CRUCES · PI YUKL, ERIK T · 2018 to 2022
$1.4M
Characterization of Accessory Factors in Bacterial Transition Metal ImportSC2GM111170 · NIGMS · NEW MEXICO STATE UNIVERSITY LAS CRUCES · PI YUKL, ERIK T · 2014 to 2016
$411k
NIGMS NIH HHS R01 GM122819NIGMS NIH HHS SC2 GM111170
6 · The paper itself

Abstract

Bacteria must acquire the essential element zinc from extremely limited environments, and this function is performed largely by ATP binding cassette (ABC) transporters. These systems rely on a periplasmic or extracellular solute binding protein (SBP) to bind zinc specifically with a high affinity and deliver it to the membrane permease for import into the cytoplasm. However, zinc acquisition systems in bacteria may be more complex, involving multiple transporters and other periplasmic or extracellular zinc binding proteins. Here we describe the zinc acquisition functions of two zinc SBPs (ZnuA and AztC) and a novel periplasmic metallochaperone (AztD) in Paracoccus denitrificans. ZnuA was characterized in vitro and demonstrated to bind as many as 5 zinc ions with a high affinity. It does not interact with AztD, in contrast to what has been demonstrated for AztC, which is able to acquire a single zinc ion through associative transfer from AztD. Deletions of the corresponding genes singly and in combination show that either AztC or ZnuA is sufficient and essential for robust growth in zinc-limited media. Although AztD cannot support transport of zinc into the cytoplasm, it likely functions to store zinc in the periplasm for transfer through the AztABCD system.

Indexed as

ATP-Binding Cassette TransportersBacterial ProteinsCalorimetryCytoplasmMetallochaperonesMutationParacoccus denitrificansPeriplasmZincATP-Binding Cassette TransportersBacterial ProteinsMetallochaperonesZinc

Identifiers

PMID30353723
PMCPMC6824839
OpenAlexW2898461816

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.