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Poplar metal tolerance protein 1 confers zinc tolerance and is an oligomeric vacuolar zinc transporter with an essential leucine zipper motif.

Identifieur interne : 004398 ( Main/Exploration ); précédent : 004397; suivant : 004399

Poplar metal tolerance protein 1 confers zinc tolerance and is an oligomeric vacuolar zinc transporter with an essential leucine zipper motif.

Auteurs : Damien Blaudez [Royaume-Uni] ; Annegret Kohler ; Francis Martin ; Dale Sanders ; Michel Chalot

Source :

RBID : pubmed:14630973

Descripteurs français

English descriptors

Abstract

Cation diffusion facilitator (CDF) proteins are a recently discovered family of cation efflux transporters that might play an essential role in metal homeostasis and tolerance. Here, we describe the identification, characterization, and localization of PtdMTP1, a member of the CDF family from the hybrid poplar Populus trichocarpa x Populus deltoides. PtdMTP1 is expressed constitutively and ubiquitously, although at low levels. Heterologous expression in yeast showed that PtdMTP1 was able to complement the hypersensitivity of mutant strains to Zn but not to other metals, including Cd, Co, Mn, and Ni. PtdMTP1 fused to green fluorescent protein localized to the vacuolar membrane both in yeast and in plant cells, consistent with a function of PtdMTP1 in zinc sequestration. Overexpression of PtdMTP1 in Arabidopsis confers Zn tolerance. We show that PtdMTP1, when expressed in yeast and Arabidopsis, forms homooligomers, a novel feature of CDF members. Oligomer formation is disrupted by reducing agents, indicating possible disulfide bridge formation. PtdMTP1 also contains a conserved Leu zipper motif. Although not necessary for oligomer formation, Leu residues within this motif are required for PtdMTP1 functional activity.

DOI: 10.1105/tpc.017541
PubMed: 14630973
PubMed Central: PMC282827


Affiliations:


Links toward previous steps (curation, corpus...)


Le document en format XML

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<term>Arabidopsis (genetics)</term>
<term>Arabidopsis (metabolism)</term>
<term>Cadmium (metabolism)</term>
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<term>Cation Transport Proteins (genetics)</term>
<term>Cation Transport Proteins (metabolism)</term>
<term>Cobalt (metabolism)</term>
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<term>Gene Expression Regulation, Plant (MeSH)</term>
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<term>Leucine Zippers (genetics)</term>
<term>Luminescent Proteins (genetics)</term>
<term>Luminescent Proteins (metabolism)</term>
<term>Manganese (metabolism)</term>
<term>Metals, Heavy (metabolism)</term>
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<term>Similitude de séquences d'acides aminés (MeSH)</term>
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<div type="abstract" xml:lang="en">Cation diffusion facilitator (CDF) proteins are a recently discovered family of cation efflux transporters that might play an essential role in metal homeostasis and tolerance. Here, we describe the identification, characterization, and localization of PtdMTP1, a member of the CDF family from the hybrid poplar Populus trichocarpa x Populus deltoides. PtdMTP1 is expressed constitutively and ubiquitously, although at low levels. Heterologous expression in yeast showed that PtdMTP1 was able to complement the hypersensitivity of mutant strains to Zn but not to other metals, including Cd, Co, Mn, and Ni. PtdMTP1 fused to green fluorescent protein localized to the vacuolar membrane both in yeast and in plant cells, consistent with a function of PtdMTP1 in zinc sequestration. Overexpression of PtdMTP1 in Arabidopsis confers Zn tolerance. We show that PtdMTP1, when expressed in yeast and Arabidopsis, forms homooligomers, a novel feature of CDF members. Oligomer formation is disrupted by reducing agents, indicating possible disulfide bridge formation. PtdMTP1 also contains a conserved Leu zipper motif. Although not necessary for oligomer formation, Leu residues within this motif are required for PtdMTP1 functional activity.</div>
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