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Published on March 11, 2009; 10.1104/pp.109.136630

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Received February 3, 2009
Accepted March 8, 2009

Physiological Roles of Glutathione S-transferases in Soybean Root Nodules

David A. Dalton *, Chris Boniface , Zachary Turner , Amy Lindahl , Hyeon Jeong Kim , Laura Jelinek , Manjula Govindarajulu , Richard E. Finger , and Christopher G. Taylor

Biology Department, Reed College, Portland, OR 97202; Donald Danforth Plant Science Center, St. Louis, MO 63132

* Corresponding author; email: david.dalton{at}reed.edu.

Glutathione S-transferases (GSTs) are ubiquitous enzymes that catalyze the conjugation of toxic xenobiotics and oxidatively produced compounds to GSH, which facilitates their metabolism, sequestration, or removal. We report here that soybean (Glycine max) root nodules contain at least 14 forms of glutathione S-transferase, with GST9 being most prevalent as measured by both real time RT-PCR and identification of peptides in glutathione-affinity purified extracts. GST8 was prevalent in stems and uninfected roots whereas GST2/10 prevailed in leaves. Purified, recombinant GSTs were shown to have wide-ranging kinetic properties, suggesting that the suite of GSTs could provide physiological flexibility to deal with numerous stresses. Levels GST9 increased with aging, suggesting a role related to senescence. RNAi studies of nodules on composite plants showed that a down regulation of GST9 led to a decrease in nitrogenase (acetylene reduction) activity and an increase in oxidatively damaged proteins. These findings indicate that GSTs are abundant in nodules and likely function to provide antioxidant defenses that are critical to support nitrogen fixation.






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