Two genes encoding Arabidopsis halleri MTP1 metal transport proteins co‐segregate with zinc tolerance and account for high MTP1 transcript levels
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Summary: The zinc hyperaccumulator plant Arabidopsis halleri is able to naturally accumulate 100‐fold higher leaf zinc concentrations when compared with non‐accumulator species such as the closely related A. lyrata and A. thaliana, without showing toxicity symptoms. A novel member of the cation diffusion facilitator (CDF) protein family, an A. halleri metal tolerance protein 1 (MTP1), and the homologous A. thaliana Zn transporter (ZAT)/AtMTP1 metal‐specifically complement the zinc hypersensitivity of a Saccharomyces cerevisiae zrc1 cot1 mutant strain. A fusion of the AhMTP1 protein to green fluorescent protein (GFP) localizes to the vacuolar membrane of A. thaliana protoplasts. When compared with A. lyrata and A. thaliana, the total MTP1 transcript levels are substantially higher in the leaves and upregulated upon exposure to high zinc concentrations in the roots of A. halleri. The high MTP1 transcript levels in A. halleri can be primarily attributed to two genetically unlinked genomic AhMTP1 gene copies. The two corresponding loci co‐segregate with zinc tolerance in the back‐cross 1 generation of a cross between the zinc‐tolerant species A. halleri and the zinc‐sensitive species A. lyrata. In contrast, a third MTP1 gene in the genome of A. halleri generates only minor amounts of MTP1 transcripts and does not co‐segregate with zinc tolerance. Our data suggests that zinc tolerance in A. halleri involves an expanded copy number of an ancestral MTP1 gene, encoding functional proteins that mediate the detoxification of zinc in the cell vacuole. At the transcript level, MTP1 gene copies of A. halleri are regulated differentially and in response to changes in zinc supply.
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MTP1 was overexpressed in A. halleri and N. caerulescens to transport Zn and Cd.
“Moreover, MTP1 was overexpressed in A. halleri and N. caerulescens to transport Zn and Cd (Dräger et al., 2004; Gustin et al., 2009).”
From Plant hyperaccumulators: a state-of-the-art review on mechanism of heavy metal transport and sequestration (2025) · cites this paper as Dräger et al., 2004
The Introduction and the section on MTP1 expression report high MTP1 transcript levels in A. halleri and a role for AhMTP1-3 in zinc detoxification. The yeast-expression results say AhMTP1-3 did not complement cadmium hypersensitivity, and this paper does not establish the claim about N. caerulescens. The cadmium-transport and N. caerulescens portions are therefore not supported by this source. (LLM, conf=0.90)
Experimental — accuracy not yet measuredIn A. halleri, the AhMTP1 gene encodes vacuolar membrane Zn/H+ antiporter, expressed 20-folds higher due to high copy number in leaves than A. thaliana.
“In A. halleri, the AhMTP1 gene encodes vacuolar membrane Zn/H+ antiporter, expressed 20-folds higher due to high copy number in leaves than A. thaliana (Becher et al., 2004; Dräger et al., 2004).”
From Plant hyperaccumulators: a state-of-the-art review on mechanism of heavy metal transport and sequestration (2025) · cites this paper as Dräger et al., 2004
The Expression section reports 14–23-fold higher MTP1 transcript signals in A. halleri shoots than in A. thaliana, and the Introduction attributes high expression to increased gene copy number and enhanced expression of two loci. The paper localizes AhMTP1-3 to the vacuolar membrane and supports a role in Zn sequestration, but it does not establish that AhMTP1 itself is a Zn/H+ antiporter; the Introduction says only that some proteins in its family may function as metal–proton antiporters. Page numbers are unavailable in our copy. (LLM, conf=0.88)
Experimental — accuracy not yet measuredDue to the higher copy number of MTP1, a Zn transporter is highly expressed in A. halleri to mediate hypertolerance.
“Due to the higher copy number of MTP1, a Zn transporter is highly expressed in A. halleri to mediate hypertolerance (Dräger et al., 2004).”
From Plant hyperaccumulators: a state-of-the-art review on mechanism of heavy metal transport and sequestration (2025) · cites this paper as Dräger et al., 2004
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- Authors
- Dräger, D. B., Desbrosses‐Fonrouge, A., Krach, C., Chardonnens, A. N., Meyer, R. C., Saumitou‐Laprade, P., & Krämer, U.
- Affiliations
- Max Planck Institute of Molecular Plant Physiology (DE)
- University of Potsdam (DE)
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Krämer, Ute
- Venue
- The Plant Journal
- Publisher
- Wiley
- Published
- 2004-07-09
- Volume
- 39
- Issue
- 3
- Pages
- 425-439
- ISSN
- 0960-7412 (ISSN-L)
- 1365-313X
- OpenAlex
- W2065437088
- Semantic Scholar
- 70fd82e656223628b75f60802041e7b1d4e02e54
- Cited by
- 294
- References
- 66
- Citations by year
- 2026: 3 · 2025: 8 · 2024: 12 · 2023: 4 · 2022: 6 · 2021: 16 · 2020: 20 · 2019: 8 · 2018: 10 · 2017: 13 · 2016: 23 · 2015: 12 · 2014: 13 · 2013: 12 · 2012: 16
- FWCI
- 20.71
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Plant Journal (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- European Commission
- Deutsche Forschungsgemeinschaft
- National Institutes of Health
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Micronutrient Interactions and Effects
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Physical Sciences › Environmental Science › Pollution › Heavy metals in environment
- Keywords
- Arabidopsis halleri, metal tolerance proteins, zinc hyperaccumulation, zinc tolerance, cation diffusion facilitator, gene copy number expansion, co-segregation, transcript regulation, backcrossing, Arabidopsis lyrata
- MeSH terms
- Amino Acid Sequence, Base Sequence, Cloning, Molecular, Crosses, Genetic, Genetic Complementation Test, Luminescent Proteins, Molecular Sequence Data, Recombinant Fusion Proteins, RNA, Messenger, Saccharomyces cerevisiae, Vacuoles, Zinc, Open Reading Frames, Genes, Plant, Arabidopsis, Sequence Homology, Amino Acid, DNA, Plant, RNA, Plant, Microsatellite Repeats, Cation Transport Proteins, Arabidopsis Proteins, Green Fluorescent Proteins
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