Towards a functional dissection of thioredoxin networks in plant cells.
Thioredoxins are a ubiquitous family of redox equivalent mediators, long considered to possess a limited number of target enzymes. Recent progress in proteomic research has allowed the identification of a wide variety of candidate proteins with which this small protein may interact in vivo. Moreover, the activity of thioredoxin itself has been recently found to be subject to regulation by posttranslational modifications, adding an additional level of complexity to the function of this intriguing enzyme family. The current review charts the technical progress made in the continuing discovery of the numerous and diverse roles played by these proteins in the regulation of redox networks in plant cells.
Hisabori
Toru
T
Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama, Japan. thisabor@res.titech.ac.jp
Motohashi
Ken
K
Hosoya-Matsuda
Naomi
N
Ueoka-Nakanishi
Hanayo
H
Romano
Patrick G N
PG
D000595:Amino Acid Sequence; D002736:Chloroplasts / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000378:metabolism; D003600:Cytosol / Q000378:metabolism; D004220:Disulfides / Q000378:metabolism; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000378:metabolism; D059828:Plant Cells; D018521:Plant Physiological Phenomena; D010944:Plants / Q000378:metabolism; D011499:Protein Processing, Post-Translational / Q000235:genetics / Q000502:physiology; D013438:Sulfhydryl Compounds / Q000378:metabolism; D013879:Thioredoxins / Q000235:genetics / Q000378:metabolism*
D004220:Disulfides; D013438:Sulfhydryl Compounds; D013879:Thioredoxins; D010088:Oxidoreductases; D003546:Cysteine Endopeptidases