title: Seed thioredoxin h.
abstract: Thioredoxins are nearly ubiquitous disulfide reductases involved in a wide range of biochemical pathways in various biological systems, and also implicated in numerous biotechnological applications. Plants uniquely synthesize an array of thioredoxins targeted to different cell compartments, for example chloroplastic f- and m-type thioredoxins involved in regulation of the Calvin-Benson cycle. The cytosolic h-type thioredoxins act as key regulators of seed germination and are recycled by NADPH-dependent thioredoxin reductase. The present review on thioredoxin h systems in plant seeds focuses on occurrence, reaction mechanisms, specificity, target protein identification, three-dimensional structure and various applications. The aim is to provide a general background as well as an update covering the most recent findings. This article is part of a Special Issue entitled: Plant Proteomics--a bridge between fundamental processes and crop production, edited by Dr. Hans-Peter Mock.
authors.affiliation: Protein and Immune Systems Biology, Department of Systems Biology, Matematiktorvet, Building 301, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark. Electronic address: ph@bio.dtu.dk.
authors.forename: Per
authors.initials: P
authors.lastname: Hägglund
authors.affiliation: Carlsberg Research Laboratory, Gamle Carlsberg Vej 4, DK-1799 Copenhagen V, Denmark.
authors.forename: Christine
authors.initials: C
authors.lastname: Finnie
authors.affiliation: National Food Research Institute, National Agriculture and Food Research Organization, Kannondai 2-1-12, Tsukuba, Ibaraki 305-8642, Japan.
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Yano
authors.affiliation: Department of Agricultural Biotechnology, College of Agriculture, Isfahan University of Technology, Isfahan 84156-83111, Iran.
authors.forename: Azar
authors.initials: A
authors.lastname: Shahpiri
authors.affiliation: Department of Plant and Microbial Biology, Koshland Hall 111, Berkeley, CA 94720-3102, USA.
authors.forename: Bob B
authors.initials: BB
authors.lastname: Buchanan
authors.affiliation: Department of Large Protein Biophysics and Formulation, Global Research Unit, Novo Nordisk A/S, Novo Nordisk Park, DK-2760 Måløv, Denmark.
authors.forename: Anette
authors.initials: A
authors.lastname: Henriksen
authors.affiliation: Enzyme and Protein Chemistry, Department of Systems Biology, Elektrovej, Building 375, DK-2800 Kgs. Lyngby, Denmark. Electronic address: bis@bio.dtu.dk.
authors.forename: Birte
authors.initials: B
authors.lastname: Svensson
mesh_terms: D018525:Germination / Q000502:physiology*; D009249:NADP / Q000378:metabolism; D010084:Oxidation-Reduction; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants / Q000378:metabolism*; D012639:Seeds / Q000378:metabolism*; D054480:Thioredoxin h / Q000378:metabolism*; D013880:Thioredoxin-Disulfide Reductase / Q000378:metabolism
chemical_list: D010940:Plant Proteins; D054480:Thioredoxin h; D009249:NADP; D013880:Thioredoxin-Disulfide Reductase
keywords: NADPH dependent thioredoxin reductase; Proteomics; Target proteins; Thioredoxin h; Three-dimensional structure