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

Marti, Maria C.; Olmos, Enrique; Calvete, Juan J.; Diaz Rodriguez, Isabel; Barranco Medina, Sergio; Whelan, James; Lazaro, Juan J.; Sevilla, Francisca y 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.

Descripción

Título: Mitochondrial and nuclear localization of a novel pea thioredoxin: identification of its mitochondrial target proteins
Autor/es:
  • Marti, Maria C.
  • Olmos, Enrique
  • Calvete, Juan J.
  • Diaz Rodriguez, Isabel
  • Barranco Medina, Sergio
  • Whelan, James
  • Lazaro, Juan J.
  • Sevilla, Francisca
  • Jimenez, Ana
Tipo de Documento: Artículo
Título de Revista/Publicación: Plant Physiology
Fecha: Junio 2009
Volumen: 150
Materias:
Escuela: E.T.S.I. Agrónomos (UPM) [antigua denominación]
Departamento: Biotecnologia [hasta 2014]
Licencias Creative Commons: Reconocimiento - Sin obra derivada - No comercial

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Resumen

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.

Más información

ID de Registro: 5098
Identificador DC: http://oa.upm.es/5098/
Identificador OAI: oai:oa.upm.es:5098
Identificador DOI: 10.1104/pp.109.138073
URL Oficial: http://www.plantphysiol.org/cgi/content/abstract/150/2/646
Depositado por: Memoria Investigacion
Depositado el: 23 Nov 2010 10:18
Ultima Modificación: 20 Abr 2016 14:03
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