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The Myristylation Motif of Pto Is Not Required for Disease Resistance

June 1998 , Volume 11 , Number  6
Pages  572 - 576

Ying-Tsu Loh , Jianmin Zhou , and Gregory B. Martin

Department of Agronomy, 1150 Lilly Hall of Life Sciences, Purdue University, West Lafayette, IN 47907-1150, U.S.A.

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Accepted 14 February 1998.

The tomato Pto kinase confers resistance to bacterial speck disease caused by strains of Pseudomonas syringae pv. tomato that express the avirulence gene avrPto. Pto contains a putative myristylation site at its amino terminus that was hypothesized to play a role in localizing Pto in the plant cell. Site-directed mutagenesis was used to change the invariant glycine residue in the myristylation motif to an alanine. Transgenes encoding the mutant Pto(G2A) and wild-type Pto were placed behind the cauliflower mosaic virus 35S promoter and transformed into tomato plants that are susceptible to bacterial speck disease. Both the mutant and wild-type forms of Pto conferred resistance to a strain of P. syringae pv. tomato expressing avrPto. These results indicate that the myristylation motif of Pto is not required for bacterial speck disease resistance.

Additional keywords: Fen, signal transduction, tyrosine kinase.

© 1998 The American Phytopathological Society