Purification and characterisation of two GST's forms from Rhizobium leguminosarum with a high affinity to herbicides.
Cytosolic glutathione transferases are a family of multifunctional proteins that catalyse the conjugation of GSH to a large variety of endogenous and exogenous compounds. These enzymes have been widely studied in mammals and, to a lesser extent, in plants. In plants, GSTs can detoxify herbicides; they are also induced by pathogenic infection and are likely to be involved in defence responses. GSTs are found in pathogenic and not pathogenic prokaryotes but the functional role played by these enzymes in the cell still remains to be clarified. Here we report the purification and characterisation of two GST forms from Rhizobium leguminosarum that play a very important role in agriculture by inducing nitrogen-fixing nodules on the roots of legumes. These bacterial GSTs from R. leguminosarum have immunological characteristics that are different among them and they are characterised both by a high affinity to herbicides.
Faraone
A
A
Department of Scienze del Farmaco, Faculty of Pharmacy, G. d'Annunzio University, Chieti, Italy.
Petrucci
M
M
Paludi
D
D
Aceto
A
A
Dainelli
B
B
D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification; D005982:Glutathione Transferase / Q000737:chemistry / Q000302:isolation & purification*; D006540:Herbicides / Q000737:chemistry / Q000494:pharmacology*; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification; D007700:Kinetics; D011485:Protein Binding; D016961:Rhizobium leguminosarum / Q000187:drug effects* / Q000201:enzymology / Q000302:isolation & purification*
D001426:Bacterial Proteins; D006540:Herbicides; D007527:Isoenzymes; D005982:Glutathione Transferase