The tomato Pto kinase confers resistance to bacterial speck disease ca
used by strains of Pseudomonas syringae pv. tomato that express the av
irulence gene avrPto. Pto contains a putative myristylation site at it
s amino terminus that was hypothesized to play a role in localizing Pt
o in the plant cell. Site-directed mutagenesis was used to change the
invariant glycine residue in the myristylation motif to an alanine. Tr
ansgenes encoding the mutant Pto(G2A) and wild-type Pto were placed be
hind the cauliflower mosaic virus 35S promoter and transformed into to
mato 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 dis
ease resistance.