title: The myristylation motif of Pto is not required for disease resistance.
abstract: 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.
authors.affiliation: Department of Agronomy, Purdue University, West Lafayette, IN 47907-1150, USA.
authors.forename: Y T
authors.initials: YT
authors.lastname: Loh
authors.forename: J
authors.initials: J
authors.lastname: Zhou
authors.forename: G B
authors.initials: GB
authors.lastname: Martin
mesh_terms: 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*
chemical_list: D017931:DNA Primers; D010940:Plant Proteins; D019814:Myristic Acid; C084354:Pto protein, Lycopersicon; D017346:Protein Serine-Threonine Kinases; D000409:Alanine; D005998:Glycine