TITLE	Thioredoxin-linked plant and animal processes: the new generation
AUTHOR	Isabelle Besse Department of Microbial and Plant Biology, University of California, Berkeley, CA 94720, USA Bob B. Buchanan Department of Microbial and Plant Biology, University of California, Berkeley, CA 94720, USA
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ABSTRACT	The renaissance in the study of thioredoxin in heterotrophic cells that began just prior to this decade has provided new insight into the function and significance of this ubiquitous regulatory disulfide protein. Thioredoxin, reduced enzymically with NADPH via NADP-thioredoxin reductase, has been found to regulate a range of biochemical processes in plants as well as animals. In so doing, thioredoxin targets intramolecular disulfide bonds of proteins such as enzyme inhibitors, seed storage proteins and enzymes. As may be seen, the target proteins have not been identified for a number of thioredoxin functions uncovered in complex systems, such as those involving transcription factors or gene inactivation. In a series of ongoing studies stemming from the fundamental work, thioredoxin has emerged as a new tool in technology and medicine. It now seems clear that we stand at a frontier in which the rapidly expanding knowledge of thioredoxin will lead to applications in industry and health.
KEYWORD	Thioredoxin; Thioredoxin reductase; Redox regulation;
ARTICLE INFO	Botanical Bulletin of Academia Sinica, Volume 38 Number 1 January 1997, page 1-11, 11 pages
PUBLISHER	Institute of Plant and Microbial Biology, Academia Sinica, Taipei, Taiwan, Republic of China