title: The Pto bacterial resistance gene and the Fen insecticide sensitivity gene encode functional protein kinases with serine/threonine specificity.
abstract: The catalytic activity and amino acid specificity of the tomato Pto and Fen kinases were investigated. The Pto and Fen genes were fused to the carboxyl terminus of the maltose-binding protein and expressed in Escherichia coli. Incubation of the purified fusion proteins with [gamma-32P]ATP in an in vitro assay showed that both proteins were capable of autophosphorylation. Mutant fusion proteins in which the conserved lysine residue of subdomain II was changed to a glutamine were unable to autophosphorylate. Phosphoamino analysis of the active fusion proteins indicated that both kinases phosphorylate serine and threonine residues but not tyrosine.
authors.affiliation: Department of Agronomy, Purdue University, West Lafayette, Indiana 47907-1150, USA.
authors.forename: Y T
authors.initials: YT
authors.lastname: Loh
authors.forename: G B
authors.initials: GB
authors.lastname: Martin
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001483:Base Sequence; D017124:Conserved Sequence; D005284:Fenthion / Q000494:pharmacology; D017343:Genes, Plant / Q000235:genetics*; D007113:Immunity, Innate / Q000235:genetics; D018551:Solanum lycopersicum / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics / Q000382:microbiology; D008969:Molecular Sequence Data; D010766:Phosphorylation; D010935:Plant Diseases / Q000235:genetics; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
chemical_list: D000596:Amino Acids; D010940:Plant Proteins; D011993:Recombinant Fusion Proteins; D005284:Fenthion; C091599:Fen protein, Lycopersicon esculentum; C084354:Pto protein, Lycopersicon; D017346:Protein Serine-Threonine Kinases