Resistance Gene and the Fen lnsecticide Encode Functional Protein Kinases with berine/Threonine Specificity’
نویسنده
چکیده
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 Escbericbia coli. lncubation of the purified fusion proteins with [y-3ZP]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 li 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.
منابع مشابه
Occur in Bacterial Speck-Susceptible and Fenthion-lnsensitive Tomato Cultivars and Encode Active Protein Kinases
The Pto gene was derived originally from the wíld tomato species Lycopersicon pimpinellifolium and confers resistance to Pseudomonas syringae pv tomato strains expressing the avirulence gene avrPto. The Fen gene is also derived from L. pimpinellifolium and confers sensitivity to the insecticide fenthion. We have now isolated and characterized the alleles of Pto and Fen from cultivated tomato, L...
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