Abstract
The protein phosphatase inhibitor, okadaic acid (OKA) increased phenylalanine ammonia lyase (PAL) activity by 30-fold in soybean ( Glycine max L.) cell suspension cultures. The increase in PAL activity was preceded by an increase in PAL mRNA. In addition, mRNA for chalcone synthase and a hydroxyproline-rich glycoprotein also increased concomitantly with PAL mRNA. In contrast, mRNA levels for the cytoskeletal proteins tubulin and actin, decreased in response to OKA treatment. The induction of the typical transcriptionally activated plant defense response to pathogens by OKA, suggests that the signal transduction pathway includes a protein phosphorylation cascade in which a protein phosphatase plays a key role.
Published Version
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