The Pto bacterial resistance gene and the Fen insecticide sensitivity gene encode functional protein kinases with serine/threonine specificity.

AUTOR(ES)

Loh, Y T

RESUMO

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.

Documentos Relacionados

• The disease-resistance gene Pto and the fenthion-sensitivity gene fen encode closely related functional protein kinases.
• Structural basis and prediction of substrate specificity in protein serine/threonine kinases
• Pim serine/threonine kinases regulate the stability of Socs-1 protein
• Eukaryotic phytochromes: Light-regulated serine/threonine protein kinases with histidine kinase ancestry
• STY, a tyrosine-phosphorylating enzyme with sequence homology to serine/threonine kinases.