Evidence map›Paper›PMID 26468286›Full record

ArticleThe Journal of biological chemistry2015

AztD, a Periplasmic Zinc Metallochaperone to an ATP-binding Cassette (ABC) Transporter System in Paracoccus denitrificans.

Melody Handali, Hridindu Roychowdhury, Durga P Neupane, Erik T Yukl

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.0field-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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Zinc-metallochaperones ofMicrobiology spectrum · 2025
    Article
  2. Structure and Function of the Zinc Binding Protein ZrgA fromInternational journal of molecular sciences · 2022
    Article
  3. Conformational flexibility in the zinc solute-binding protein ZnuA.Acta crystallographica. Section F, Structural biology communications · 2022
    Article
  4. Article
  5. Article
  6. Oligopeptide-binding protein from nontypeableThe Journal of biological chemistry · 2019
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Zinc-Dependent Transcriptional Regulation inFrontiers in microbiology · 2017
    Article
  12. The biological inorganic chemistry of zinc ions.Archives of biochemistry and biophysics · 2016
    Article
  13. 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

4 authors at 1 institution in 1 country.

Melody HandaliFrom the Department of Chemistry and Biochemistry, New Mexico State University, Las Cruces, New Mexico 88003.
Hridindu RoychowdhuryFrom the Department of Chemistry and Biochemistry, New Mexico State University, Las Cruces, New Mexico 88003.
Durga P NeupaneFrom the Department of Chemistry and Biochemistry, New Mexico State University, Las Cruces, New Mexico 88003.
Erik T YuklFrom the Department of Chemistry and Biochemistry, New Mexico State University, Las Cruces, New Mexico 88003 etyukl@nmsu.edu.
New Mexico State University · US

Funding

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 1SC2GM111170-01NIGMS NIH HHS SC2 GM111170
6 · The paper itself

Abstract

Bacterial ATP-binding cassette (ABC) transporters of transition metals are essential for acquisition of necessary elements from the environment. A large number of Gram-negative bacteria, including human pathogens, have a fourth conserved gene of unknown function adjacent to the canonical permease, ATPase, and solute-binding protein (SBP) genes of the AztABC zinc transporter system. To assess the function of this putative accessory factor (AztD) from Paracoccus denitrificans, we have analyzed its transcriptional regulation, metal binding properties, and interaction with the SBP (AztC). Transcription of the aztD gene is significantly up-regulated under conditions of zinc starvation. Recombinantly expressed AztD purifies with slightly substoichiometric zinc from the periplasm of Escherichia coli and is capable of binding up to three zinc ions with high affinity. Size exclusion chromatography and a simple intrinsic fluorescence assay were used to determine that AztD as isolated is able to transfer bound zinc nearly quantitatively to apo-AztC. Transfer occurs through a direct, associative mechanism that prevents loss of metal to the solvent. These results indicate that AztD is a zinc chaperone to AztC and likely functions to maintain zinc homeostasis through interaction with the AztABC system. This work extends our understanding of periplasmic zinc trafficking and the function of chaperones in this process.

Indexed as

ATP-Binding Cassette TransportersBacterial ProteinsCircular DichroismMolecular ChaperonesParacoccus denitrificansPeriplasmProtein BindingSpectrometry, FluorescenceZincATP-Binding Cassette TransportersBacterial ProteinsMolecular ChaperonesZincABC transporterchaperonemetal homeostasismetalloproteinzinc

Identifiers

PMID26468286
PMCPMC4705993
OpenAlexW2195806069

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.