Evidence map›Paper›PMID 22139846›Full record

ArticleThe Journal of biological chemistry2012

Metal selectivity determinants in a family of transition metal transporters.

Dorina Podar, Judith Scherer, Zeenat Noordally, Pawel Herzyk, Dietrich Nies, Dale Sanders

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.8field-weighted citation impact, top 5% 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

46 citing papers in PubMed, 111 citations in OpenAlex.

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  12. Mechanism of Zinc Transport through the Zinc Transporter YiiP.Journal of chemical theory and computation · 2022
    Article
  13. Genetic determinants of micronutrient traits in graminaceous crops to combat hidden hunger.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2021
    Review
  14. Comparative and Systematic Omics Revealed Low Cd Accumulation of PotatoInternational journal of molecular sciences · 2021
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 4 institutions in 3 countries.

Dorina PodarDepartment of Biology, University of York, York YO10 5DD, United Kingdom. dorina.podar@gmail.com
Judith Scherer
Zeenat Noordally
Pawel Herzyk
Dietrich Nies
Dale Sanders
Martin Luther University Halle-Wittenberg · DEUniversity of York · GBJohn Innes Centre · GBUniversity of Glasgow · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Metal tolerance proteins (MTPs) are plant members of the cation diffusion facilitator (CDF) transporter family involved in cellular metal homeostasis. Members of the CDF family are ubiquitously found in all living entities and show principal selectivity for Zn(2+), Mn(2+), and Fe(2+). Little is known regarding metal selectivity determinants of CDFs. We identified a novel cereal member of CDFs in barley, termed HvMTP1, that localizes to the vacuolar membrane. Unlike its close relative AtMTP1, which is highly selective for Zn(2+), HvMTP1 exhibits selectivity for both Zn(2+) and Co(2+) as assessed by its ability to suppress yeast mutant phenotypes for both metals. Expression of HvMTP1/AtMTP1 chimeras in yeast revealed a five-residue sequence within the AtMTP1 N-segment of the His-rich intracytoplasmic loop that confines specificity to Zn(2+). Furthermore, mutants of AtMTP1 generated through random mutagenesis revealed residues embedded within transmembrane domain 3 that additionally specify the high degree of Zn(2+) selectivity. We propose that the His-rich loop, which might play a role as a zinc chaperone, determines the identity of the metal ions that are transported. The residues within transmembrane domain 3 can also influence metal selectivity, possibly through conformational changes induced at the cation transport site located within the membrane or at the cytoplasmic C-terminal domain.

Indexed as

ArabidopsisArabidopsis ProteinsCation Transport ProteinsHordeumIon TransportMetalsProtein Structure, SecondaryProtein Structure, TertiaryRecombinant Fusion ProteinsSaccharomyces cerevisiaeVacuolesArabidopsis ProteinsCation Transport ProteinsMetalsRecombinant Fusion ProteinsZAT protein, Arabidopsis

Identifiers

PMID22139846
PMCPMC3270973
OpenAlexW2087371433

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.