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Plant homologs of the Plasmodium falciparum chloroquine-resistance transporter, PfCRT, are required for glutathione homeostasis and stress responses.

Identifieur interne : 001857 ( Main/Exploration ); précédent : 001856; suivant : 001858

Plant homologs of the Plasmodium falciparum chloroquine-resistance transporter, PfCRT, are required for glutathione homeostasis and stress responses.

Auteurs : Spencer C. Maughan [Royaume-Uni] ; Maciej Pasternak ; Narelle Cairns ; Guy Kiddle ; Thorsten Brach ; Renee Jarvis ; Florian Haas ; Jeroen Nieuwland ; Benson Lim ; Christopher Müller ; Enrique Salcedo-Sora ; Cordula Kruse ; Mathilde Orsel ; Rüdiger Hell ; Anthony J. Miller ; Patrick Bray ; Christine H. Foyer ; James A H. Murray ; Andreas J. Meyer ; Christopher S. Cobbett

Source :

RBID : pubmed:20080670

Descripteurs français

English descriptors

Abstract

In Arabidopsis thaliana, biosynthesis of the essential thiol antioxidant, glutathione (GSH), is plastid-regulated, but many GSH functions, including heavy metal detoxification and plant defense activation, depend on cytosolic GSH. This finding suggests that plastid and cytosol thiol pools are closely integrated and we show that in Arabidopsis this integration requires a family of three plastid thiol transporters homologous to the Plasmodium falciparum chloroquine-resistance transporter, PfCRT. Arabidopsis mutants lacking these transporters are heavy metal-sensitive, GSH-deficient, and hypersensitive to Phytophthora infection, confirming a direct requirement for correct GSH homeostasis in defense responses. Compartment-specific measurements of the glutathione redox potential using redox-sensitive GFP showed that knockout of the entire transporter family resulted in a more oxidized glutathione redox potential in the cytosol, but not in the plastids, indicating the GSH-deficient phenotype is restricted to the cytosolic compartment. Expression of the transporters in Xenopus oocytes confirmed that each can mediate GSH uptake. We conclude that these transporters play a significant role in regulating GSH levels and the redox potential of the cytosol.

DOI: 10.1073/pnas.0913689107
PubMed: 20080670
PubMed Central: PMC2836691


Affiliations:


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Le document en format XML

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<term>Antimalarials (pharmacology)</term>
<term>Arabidopsis (genetics)</term>
<term>Arabidopsis (metabolism)</term>
<term>Arabidopsis Proteins (genetics)</term>
<term>Arabidopsis Proteins (metabolism)</term>
<term>Cadmium (pharmacology)</term>
<term>Chloroquine (pharmacology)</term>
<term>Drug Resistance (MeSH)</term>
<term>Female (MeSH)</term>
<term>Genes, Plant (MeSH)</term>
<term>Glutathione (metabolism)</term>
<term>Homeostasis (MeSH)</term>
<term>In Vitro Techniques (MeSH)</term>
<term>Membrane Transport Proteins (genetics)</term>
<term>Membrane Transport Proteins (metabolism)</term>
<term>Models, Biological (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Oocytes (metabolism)</term>
<term>Plants, Genetically Modified (MeSH)</term>
<term>Plasmodium falciparum (drug effects)</term>
<term>Plasmodium falciparum (genetics)</term>
<term>Plasmodium falciparum (metabolism)</term>
<term>Protozoan Proteins (genetics)</term>
<term>Protozoan Proteins (metabolism)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>Stress, Physiological (MeSH)</term>
<term>Xenopus (MeSH)</term>
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<term>Animaux (MeSH)</term>
<term>Antipaludiques (pharmacologie)</term>
<term>Arabidopsis (génétique)</term>
<term>Arabidopsis (métabolisme)</term>
<term>Cadmium (pharmacologie)</term>
<term>Chloroquine (pharmacologie)</term>
<term>Femelle (MeSH)</term>
<term>Glutathion (métabolisme)</term>
<term>Gènes de plante (MeSH)</term>
<term>Homéostasie (MeSH)</term>
<term>Modèles biologiques (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Ovocytes (métabolisme)</term>
<term>Plasmodium falciparum (effets des médicaments et des substances chimiques)</term>
<term>Plasmodium falciparum (génétique)</term>
<term>Plasmodium falciparum (métabolisme)</term>
<term>Protéines d'Arabidopsis (génétique)</term>
<term>Protéines d'Arabidopsis (métabolisme)</term>
<term>Protéines de protozoaire (génétique)</term>
<term>Protéines de protozoaire (métabolisme)</term>
<term>Protéines de transport membranaire (génétique)</term>
<term>Protéines de transport membranaire (métabolisme)</term>
<term>Protéines recombinantes (génétique)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Résistance aux substances (MeSH)</term>
<term>Stress physiologique (MeSH)</term>
<term>Techniques in vitro (MeSH)</term>
<term>Végétaux génétiquement modifiés (MeSH)</term>
<term>Xenopus (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en">
<term>Arabidopsis Proteins</term>
<term>Membrane Transport Proteins</term>
<term>Protozoan Proteins</term>
<term>Recombinant Proteins</term>
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<term>Arabidopsis Proteins</term>
<term>Glutathione</term>
<term>Membrane Transport Proteins</term>
<term>Protozoan Proteins</term>
<term>Recombinant Proteins</term>
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<term>Antimalarials</term>
<term>Cadmium</term>
<term>Chloroquine</term>
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<keywords scheme="MESH" qualifier="drug effects" xml:lang="en">
<term>Plasmodium falciparum</term>
</keywords>
<keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr">
<term>Plasmodium falciparum</term>
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<term>Arabidopsis</term>
<term>Plasmodium falciparum</term>
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<term>Arabidopsis</term>
<term>Plasmodium falciparum</term>
<term>Protéines d'Arabidopsis</term>
<term>Protéines de protozoaire</term>
<term>Protéines de transport membranaire</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en">
<term>Arabidopsis</term>
<term>Oocytes</term>
<term>Plasmodium falciparum</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr">
<term>Arabidopsis</term>
<term>Glutathion</term>
<term>Ovocytes</term>
<term>Plasmodium falciparum</term>
<term>Protéines d'Arabidopsis</term>
<term>Protéines de protozoaire</term>
<term>Protéines de transport membranaire</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr">
<term>Antipaludiques</term>
<term>Cadmium</term>
<term>Chloroquine</term>
</keywords>
<keywords scheme="MESH" xml:lang="en">
<term>Animals</term>
<term>Drug Resistance</term>
<term>Female</term>
<term>Genes, Plant</term>
<term>Homeostasis</term>
<term>In Vitro Techniques</term>
<term>Models, Biological</term>
<term>Mutation</term>
<term>Plants, Genetically Modified</term>
<term>Stress, Physiological</term>
<term>Xenopus</term>
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<term>Animaux</term>
<term>Femelle</term>
<term>Gènes de plante</term>
<term>Homéostasie</term>
<term>Modèles biologiques</term>
<term>Mutation</term>
<term>Résistance aux substances</term>
<term>Stress physiologique</term>
<term>Techniques in vitro</term>
<term>Végétaux génétiquement modifiés</term>
<term>Xenopus</term>
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<front>
<div type="abstract" xml:lang="en">In Arabidopsis thaliana, biosynthesis of the essential thiol antioxidant, glutathione (GSH), is plastid-regulated, but many GSH functions, including heavy metal detoxification and plant defense activation, depend on cytosolic GSH. This finding suggests that plastid and cytosol thiol pools are closely integrated and we show that in Arabidopsis this integration requires a family of three plastid thiol transporters homologous to the Plasmodium falciparum chloroquine-resistance transporter, PfCRT. Arabidopsis mutants lacking these transporters are heavy metal-sensitive, GSH-deficient, and hypersensitive to Phytophthora infection, confirming a direct requirement for correct GSH homeostasis in defense responses. Compartment-specific measurements of the glutathione redox potential using redox-sensitive GFP showed that knockout of the entire transporter family resulted in a more oxidized glutathione redox potential in the cytosol, but not in the plastids, indicating the GSH-deficient phenotype is restricted to the cytosolic compartment. Expression of the transporters in Xenopus oocytes confirmed that each can mediate GSH uptake. We conclude that these transporters play a significant role in regulating GSH levels and the redox potential of the cytosol.</div>
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<AbstractText>In Arabidopsis thaliana, biosynthesis of the essential thiol antioxidant, glutathione (GSH), is plastid-regulated, but many GSH functions, including heavy metal detoxification and plant defense activation, depend on cytosolic GSH. This finding suggests that plastid and cytosol thiol pools are closely integrated and we show that in Arabidopsis this integration requires a family of three plastid thiol transporters homologous to the Plasmodium falciparum chloroquine-resistance transporter, PfCRT. Arabidopsis mutants lacking these transporters are heavy metal-sensitive, GSH-deficient, and hypersensitive to Phytophthora infection, confirming a direct requirement for correct GSH homeostasis in defense responses. Compartment-specific measurements of the glutathione redox potential using redox-sensitive GFP showed that knockout of the entire transporter family resulted in a more oxidized glutathione redox potential in the cytosol, but not in the plastids, indicating the GSH-deficient phenotype is restricted to the cytosolic compartment. Expression of the transporters in Xenopus oocytes confirmed that each can mediate GSH uptake. We conclude that these transporters play a significant role in regulating GSH levels and the redox potential of the cytosol.</AbstractText>
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<GrantID>BBS/E/C/00004166</GrantID>
<Agency>Biotechnology and Biological Sciences Research Council</Agency>
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<Grant>
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<Agency>Biotechnology and Biological Sciences Research Council</Agency>
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<Grant>
<GrantID>BB/C51508X/1</GrantID>
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