Evidence map›Paper›PMID 23761487›Full record

ArticleJournal of experimental botany2013

Functional analysis of the rice vacuolar zinc transporter OsMTP1.

Paloma K Menguer, Emily Farthing, Kerry A Peaston, Felipe Klein Ricachenevsky, Janette Palma Fett, Lorraine E Williams

Open access · hybridAbstract read
In one paragraph

Article in Journal of experimental botany, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed, 1 pooled it
10.2field-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

58 citing papers in PubMed, 1 synthesis or guideline pooled it, 173 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. From paddy soil to dining table: biological biofortification of rice with zinc.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2026
    Review
  6. Article
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  8. Review
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  10. Article
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  15. Review
  16. Article
  17. Article
  18. Article
  19. MTP8 fromInternational journal of molecular sciences · 2022
    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

6 authors at 2 institutions in 2 countries.

Paloma K MenguerCentre for Biological Science, University of Southampton, Life Sciences Building 85, Highfield Campus, Southampton SO17 1B, UK.
Emily Farthing
Kerry A Peaston
Felipe Klein Ricachenevsky
Janette Palma Fett
Lorraine E Williams
Universidade Federal do Rio Grande do Sul · BRUniversity of Southampton · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heavy metal homeostasis is maintained in plant cells by specialized transporters which compartmentalize or efflux metal ions, maintaining cytosolic concentrations within a narrow range. OsMTP1 is a member of the cation diffusion facilitator (CDF)/metal tolerance protein (MTP) family of metal cation transporters in Oryza sativa, which is closely related to Arabidopsis thaliana MTP1. Functional complementation of the Arabidopsis T-DNA insertion mutant mtp1-1 demonstrates that OsMTP1 transports Zn in planta and localizes at the tonoplast. When heterologously expressed in the yeast mutant zrc1 cot1, OsMTP1 complemented its Zn hypersensitivity and was also localized to the vacuole. OsMTP1 alleviated, to some extent, the Co sensitivity of this mutant, rescued the Fe hypersensitivity of the ccc1 mutant at low Fe concentrations, and restored growth of the Cd-hypersensitive mutant ycf1 at low Cd concentrations. These results suggest that OsMTP1 transports Zn but also Co, Fe, and Cd, possibly with lower affinity. Site-directed mutagenesis studies revealed two substitutions in OsMTP1 that alter the transport function of this protein. OsMTP1 harbouring a substitution of Leu82 to a phenylalanine can still transport low levels of Zn, with an enhanced affinity for Fe and Co, and a gain of function for Mn. A substitution of His90 with an aspartic acid completely abolishes Zn transport but improves Fe transport in OsMTP1. These amino acid residues are important in determining substrate specificity and may be a starting point for refining transporter activity in possible biotechnological applications, such as biofortification and phytoremediation.

Indexed as

Amino Acid SequenceCation Transport ProteinsMetals, HeavyMolecular Sequence DataMutagenesis, Site-DirectedOryzaPhylogenyPlant ProteinsProtein TransportSequence AlignmentVacuolesZincCation Transport ProteinsMetals, HeavyPlant ProteinsZincCation diffusion facilitatorion selectivitymetal tolerance proteinOryza sativavacuolezinc transporter.

Identifiers

PMID23761487
PMCPMC3697945
OpenAlexW2148699164

What OpenQuestion holds

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LicenceCC BY-NC
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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.