The reduced form of glutathione (GSH), when supplied to suspension cultured cells of bean (Phaseolus vulgaris L.) at concentrations in the range 0.01 to 1.0 millimolar, stimulates transcription of defense genes including those that encode cel wall hydroxyproline-rich glycoproteins and the phenylpropanoid biosynthetic enzymes phenylalanine ammonialyase (PAL) and chalcone synthase (CHS) involved in lignin (PAL) and phytoalexin (PAL, CHS) production. Transcriptional activation of these genes leads to marked accumulation of the corresponding transcripts, contributing to a massive change in the overall pattern of protein synthesis which closely resembles that previously observed in response to fungal elicitor. GSH causes a marked increase in extractable PAL activity, whereas the oxidized form of glutathione, constituent amino acids, or other reducing agents are inactive. Possible roles of GSH in signaling biological stress are discussed.Glutathione (y-L-glutamyl-L-cysteinyl-glycine) is a low mol wt thiol implicated in a wide range of metabolic processes (16). Functions proposed for glutathione in higher plants include: storage and transport of reduced sulfur; protein reductant; destruction of H202 in chloroplasts, and detoxification of xenobiotics including certain herbicides and pesticides (8,20). Overall, glutathione appears to play a key role in protection against oxidative damage arising from a number of stresses such as irradiation (16), heat (18), and exposure to heavy metals (10).Redox perturbations including generation of superoxide anions and lipid peroxidation appear to be a characteristic response to mechanical damage and microbial infection (4). Moreover, certain sulfhydryl reagents stimulate the production of phytoalexins and the activation of other defense responses associated with the expression of disease resistance (11,24). Taken