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

Marti, Maria C. and Olmos, Enrique and Calvete, Juan J. and Diaz Rodriguez, Isabel and Barranco Medina, Sergio and Whelan, James and Lazaro, Juan J. and Sevilla, Francisca and Jimenez, Ana (2009). Mitochondrial and nuclear localization of a novel pea thioredoxin: identification of its mitochondrial target proteins. "Plant Physiology", v. 150 ; pp. 646-657. ISSN 0032-0889. https://doi.org/10.1104/pp.109.138073.

Description

Title: Mitochondrial and nuclear localization of a novel pea thioredoxin: identification of its mitochondrial target proteins
Author/s:
  • Marti, Maria C.
  • Olmos, Enrique
  • Calvete, Juan J.
  • Diaz Rodriguez, Isabel
  • Barranco Medina, Sergio
  • Whelan, James
  • Lazaro, Juan J.
  • Sevilla, Francisca
  • Jimenez, Ana
Item Type: Article
Título de Revista/Publicación: Plant Physiology
Date: June 2009
ISSN: 0032-0889
Volume: 150
Subjects:
Faculty: E.T.S.I. Agrónomos (UPM) [antigua denominación]
Department: Biotecnologia [hasta 2014]
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

Plants contain several genes encoding thioredoxins (Trxs), small proteins involved in the regulation of the activity of many enzymes through dithiol-disulfide exchange. In addition to chloroplastic and cytoplasmic Trx systems, plant mitochondria contain a reduced nicotinamide adenine dinucleotide phosphate-dependent Trx reductase 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) mitochondria and nuclei of a Trx isoform (PsTrxo1) that seems to belong to the Trx o group, although it differs from this Trx type by its absence of introns in the genomic sequence. Western-blot analysis with isolated mitochondria and nuclei, immunogold labeling, and green fluorescent protein fusion constructs all indicated that PsTrxo1 is present in both cell compartments. Moreover, the identification by tandem mass spectrometry of the native mitochondrial Trx after gel filtration using the fast-protein liquid chromatography 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 cerevisiae mitochondrial Trx reductase Trr2 than by the wheat (Triticum aestivum) cytoplasmic reduced nicotinamide adenine dinucleotide phosphate-dependent Trx reductase. 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.

More information

Item ID: 5098
DC Identifier: http://oa.upm.es/5098/
OAI Identifier: oai:oa.upm.es:5098
DOI: 10.1104/pp.109.138073
Official URL: http://www.plantphysiol.org/cgi/content/abstract/150/2/646
Deposited by: Memoria Investigacion
Deposited on: 23 Nov 2010 10:18
Last Modified: 20 Apr 2016 14:03
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