Copper transporter COPT5 participates in the crosstalk between vacuolar copper and iron pools mobilisation.


Journal

Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288

Informations de publication

Date de publication:
15 03 2019
Historique:
received: 03 08 2018
accepted: 17 12 2018
entrez: 16 3 2019
pubmed: 16 3 2019
medline: 2 10 2020
Statut: epublish

Résumé

Copper (Cu) deficiency affects iron (Fe) homeostasis in several plant processes, including the increased Fe requirements due to cuproprotein substitutions for the corresponding Fe counterpart. Loss-of-function mutants from Arabidopsis thaliana high affinity copper transporter COPT5 and Fe transporters NATURAL RESISTANCE-ASSOCIATED MACROPHAGE PROTEIN 3/4 (NRAMP3 and NRAMP4) were used to study the interaction between metals internal pools. A physiological characterisation showed that the copt5 mutant is sensitive to Fe deficiency, and that nramp3nramp4 mutant growth was severely affected under limiting Cu. By a transcriptomic analysis, we observed that NRAMP4 expression was highly induced in the copt5 mutant under Cu deficiency, while COPT5 was overexpressed in the nramp3nramp4 mutant. As a result, an enhanced mobilisation of the vacuolar Cu or Fe pools, when the other metal export through the tonoplast is impaired in the mutants, has been postulated. However, metals coming from internal pools are not used to accomplish the increased requirements that derive from metalloprotein substitution under metal deficiencies. Instead, the metal concentrations present in aerial parts of the copt5 and nramp3nramp4 mutants conversely show compensated levels of these two metals. Together, our data uncover an interconnection between Cu and Fe vacuolar pools, whose aim is to fulfil interorgan metal translocation.

Identifiants

pubmed: 30874615
doi: 10.1038/s41598-018-38005-4
pii: 10.1038/s41598-018-38005-4
pmc: PMC6420658
doi:

Substances chimiques

Arabidopsis Proteins 0
COPT5 protein, Arabidopsis 0
Copper Transport Proteins 0
Metals 0
SLC31 Proteins 0
Copper 789U1901C5
Iron E1UOL152H7

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

4648

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Auteurs

Àngela Carrió-Seguí (À)

Departament de Bioquímica i Biologia Molecular and ERI Biotecmed, Universitat de València, Av. Doctor Moliner, 50, ES-46100, Burjassot, Valencia, Spain.
Instituto de Biología Molecular y Celular de Plantas (CSIC-Universidad Politécnica de Valencia), C/Ingeniero Fausto Elio, s/n. 46022, Valencia, Spain.

Paco Romero (P)

Departament de Bioquímica i Biologia Molecular and ERI Biotecmed, Universitat de València, Av. Doctor Moliner, 50, ES-46100, Burjassot, Valencia, Spain.
Department of Food Biotechnology, Institute of Agrochemistry and Food Technology (IATA-CSIC), Av. Agustin Escardino, 7, 46980, Paterna, Valencia, Spain.

Catherine Curie (C)

Laboratoire de Biochimie et Physiologie Moléculaire des Plantes, Institut de Biologie Intégrative des Plantes, Centre National de la Recherche Scientifique (UMR5004), Institut National de la Recherche Agronomique, Université Montpellier II, Ecole Nationale Supérieure d'Agronomie, 34060, Montpellier Cedex 2, France.

Stéphane Mari (S)

Laboratoire de Biochimie et Physiologie Moléculaire des Plantes, Institut de Biologie Intégrative des Plantes, Centre National de la Recherche Scientifique (UMR5004), Institut National de la Recherche Agronomique, Université Montpellier II, Ecole Nationale Supérieure d'Agronomie, 34060, Montpellier Cedex 2, France.

Lola Peñarrubia (L)

Departament de Bioquímica i Biologia Molecular and ERI Biotecmed, Universitat de València, Av. Doctor Moliner, 50, ES-46100, Burjassot, Valencia, Spain. lola.penarrubia@uv.es.

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Classifications MeSH