Protein dephosphorylation mediates salicylic acid‐induced expression of PR‐1 genes in tobacco

Abstract

Several lines of evidence suggest that salicylic acid (SA) is an endogenous signal for the activation of several plant defense responses, including the expression of genes encoding pathogenesis‐related (PR) proteins such as the acidic PR‐1 proteins. During recent years, studies have suggested that interaction of SA with catalase and ascorbate peroxidase leads to two signals in tobacco ‐ elevated H2O2 levels and lipid peroxides. However, to date, relatively little is known about the molecular and biochemical mechanisms that mediate transduction beyond these signals or through other SA‐effector proteins. Using protein kinase and phosphatase inhibitors, this study demonstrates that PR‐1 gene induction can be mediated by dephosphorylation of serine/threonine residue(s) of two or more unidentified phosphoproteins. The protein phosphatase inhibitors, okadaic acid and calyculin A blocked SA‐mediated induction of PR‐1 genes, implying the involvement of a phosphoprotein downstream of SA. The protein kinase inhibitors K‐252a and staurosporine induced PR‐1 gene expression. PR‐1 gene induction by K‐252a was suppressed by okadaic acid. Surprisingly, this induction was also suppressed in NahG transgenic tobacco plants which convert SA to catechol. Moreover, K‐252a stimulated production of SA and its glucoside, suggesting that another phosphoprotein acts upstream of SA. Taken together, these results suggest that there are two (or more) phosphoproteins which function in the same signal transduction pathway leading to PR‐1 gene induction. The SA‐inducible acidic PR‐2 genes were similarly affected by the inhibitors, while the genes for actin and phenylalanine ammonia lyase were not.