title: Plant thioredoxins: the multiplicity conundrum.
abstract: Thioredoxins are small proteins distinguished by the presence of a conserved dicysteine active site. In oxidized thioredoxin, the two cysteines form a disulfide bond that is targeted by the enzyme thioredoxin reductase. Together with an electron donor, thioredoxin and thioredoxin reductase form the 'thioredoxin system' that is present in all organisms. Thioredoxins participate in dithiol/disulfide exchange reactions with a large range of cellular substrates. Higher plants possess a very complex thioredoxin profile consisting of at least two different thioredoxin systems that contain distinct, multigenic thioredoxin classes which have different intracellular localizations. In this review we summarise the current state of knowledge regarding the function of plant thioredoxins representing all systems and classes.
authors.affiliation: University of Adelaide, Waite Agricultural Research Institute, Department of Plant Science, Glen Osmond, South Australia, Australia. ubaumann@waite.adelaide.edu.au
authors.forename: U
authors.initials: U
authors.lastname: Baumann
authors.forename: J
authors.initials: J
authors.lastname: Juttner
mesh_terms: D000595:Amino Acid Sequence; D019143:Evolution, Molecular; D008969:Molecular Sequence Data; D005810:Multigene Family; D018521:Plant Physiological Phenomena; D011487:Protein Conformation; D013880:Thioredoxin-Disulfide Reductase / Q000502:physiology; D013879:Thioredoxins / Q000235:genetics
chemical_list: D013879:Thioredoxins; D013880:Thioredoxin-Disulfide Reductase