The myristylation motif of Pto is not required for disease resistance.
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.
Loh
Y T
YT
Department of Agronomy, Purdue University, West Lafayette, IN 47907-1150, USA.
Zhou
J
J
Martin
G B
GB
D000409:Alanine / Q000378:metabolism; D000595:Amino Acid Sequence; D001483:Base Sequence; D017796:Caulimovirus / Q000235:genetics; D017931:DNA Primers; D005998:Glycine / Q000378:metabolism; D018551:Solanum lycopersicum / Q000201:enzymology; D016297:Mutagenesis, Site-Directed; D019814:Myristic Acid / Q000378:metabolism*; D010940:Plant Proteins; D030821:Plants, Genetically Modified; D011401:Promoter Regions, Genetic; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism*
D017931:DNA Primers; D010940:Plant Proteins; D019814:Myristic Acid; C084354:Pto protein, Lycopersicon; D017346:Protein Serine-Threonine Kinases; D000409:Alanine; D005998:Glycine