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Published on April 10, 2009; 10.1104/pp.109.138073

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Received March 4, 2009
Accepted April 6, 2009

Mitochondrial and nuclear localization of a novel pea thioredoxin: identification of its mitochondrial target proteins

Maria C. Marti , Enrique Olmos , Juan J. Calvete , Isabel Diaz , Sergio Barranco-Medina , James Whelan , Juan J. Lazaro , Francisca Sevilla , and Ana Jimenez *

Department of Stress Biology and Plant Pathology, Centro de Edafologia y Biologia Aplicada del Segura, CSIC, P.O. Box 164, E-30100, Murcia, Spain; Laboratory of Structural Proteomic, Instituto de Biomedicina, CSIC, E-46010, Valencia, Spain; Department of Biotechnology, ETSIA-UPM, E-28040, Madrid, Spain; Department of Biochemistry, Cellular and Molecular Biology of Plants, Estacion Experimental del Zaidin, CSIC, P.O. Box 419, E-18080 Granada, Spain; ARC Centre of Excellence in Plant Energy Biology, University of Western Australia, Crawley 6009, Western Australia, Australia

* Corresponding author; email: ajimenez{at}cebas.csic.es.

Plants contain several genes encoding thioredoxins (Trx), small proteins involved in the regulation of the activity of many enzymes through dithiol-disulphide exchange. In addition to chloroplastic and cytoplasmic Trx systems, plant mitochondria contain an NADPH-dependent Trx reductase (NTR) and a specific Trx o and to date, there have been no reports of a gene encoding a plant nuclear Trx. We report here the presence in pea (Pisum sativum L.) mitochondria and nuclei of a thioredoxin isoform (PsTrxo1) which seems to belong to the thioredoxin o group, although it differs from this thioredoxin type by its absence of introns in the genomic sequence. Western blot analysis with isolated mitochondria and nuclei, immunogold labelling and GFP fusion constructs all indicated that PsTrxo1 is present to both cell compartments. Moreover, the identification by MS/MS of the native mitochondrial thioredoxin after gel filtration using FPLC system of highly purified mitochondria, and the in vitro uptake assay into isolated mitochondria also corroborated a mitochondrial location for this protein. The recombinant PsTrxo1 protein has been shown to be reduced more effectively by the Saccharomyces cerevesiae mitochondrial thioredoxin reductase Trr2 than by the wheat cytoplasmic NTR. PsTrxo1 was able to activate alternative oxidase and it was shown to interact with a number of mitochondrial proteins, including peroxiredoxin and enzymes mainly involved in the photorespiratory process.






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