The role of GSTs in the tolerance of Rhizobium leguminosarum to cadmium. 
A high intraspecific difference in cadmium (Cd) tolerance exits among Rhizobium leguminosarum strains.  The higher tolerance to Cd appeared to be related to the efficiency of the glutathione (GSH)-Cd chelation mechanism, but it is not known how efficiency is influenced.  Thus, in this work it was intended to investigate the traits behind the efficiency of intracellular Cd chelation by GSH.  Glutathione-S-transferases (GST; EC 2.5.1.18) are a family of multi-functional dimeric proteins, found in both prokaryotes and eukaryotes, which are implicated in a variety of stress conditions.  The common feature of these enzymes is to catalyze the conjugation of the sulfur atom of GSH with a large variety of hydrophobic toxic compounds of both endogenous and exogenous origin.  Taking into account the reactions catalyzed by GSTs, it was hypothesized that they could be involved in the GSH-Cd complex formation in R. leguminosarum.  Differences in GSTs activity between strains could explain variation in Cd chelation efficiency detected among strains and, consequently, discrepancy in tolerance to Cd.  Thus, GST isoforms of R. leguminosarum strains with distinct tolerances to Cd were purified and their activity investigated.  The relationship between chelation efficiency and enzymatic activity of GSTs was demonstrated, supporting the hypothesis that GSTs, in particular one isoform, was involved in the formation of GSH-Cd complexes and in the tolerance of Rhizobium to Cd.