Characterization of a 34-kDa soybean binding protein for the syringolide elicitors

Syringolides are water-soluble, low-molecular-weight elicitors that trigger defense responses in soybean cultivars carrying the Rpg4 disease-resistance gene but not in rpg4 cultivars, I-125-syringolide 1 previously was shown to bind to a soluble protein(s) in extracts from soybean leaves, A 34-kDa protein that accounted for I-125-syringolide 1 binding activity was isolated with a syringolide affinity-gel column, Partial sequences of internal peptides of the 34-kDa protein were identical to P34, a previously described soybean seed allergen, In soybean seeds, P34 is processed from a 46-kDa precursor protein and was shown to have homology with thiol proteases, P34 is a moderately abundant protein in soybean seeds and cotyledons but its level in leaves is low, cDNAs encoding 46-, 34-, and 32-kDa forms of the soybean protein were cloned into the baculovirus vector, pVL1392, and expressed in insect cells, The resulting 32- and 34-kDa proteins, but not the 46-kDa protein, exhibited ligand-specific I-125-syringolide binding activity, These results suggest that P34 may be the receptor that mediates syringolide signaling.