The major site of the Pti1 kinase phosphorylated by the Pto kinase is located in the activation domain and is required for Pto-Pti1 physical interaction

European Journal of Biochemistry

Volumn 267, Issue 1, 2000, Pages 171-178

  Sessa, Guido ^a   D'Ascenzo, Mark ^a   Martin, Gregory B ^a  

^a United States Department of Agriculture Agricultural Research Service and Boyce Thompson Institute for Plant Research   (United States)

Author keywords

Disease resistance; Phosphorylation; Pti1; Pto; Tomato

Indexed keywords

ALANINE; ASPARTIC ACID; BETA GALACTOSIDASE; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; MALTOSE BINDING PROTEIN; PHOSPHOAMINO ACID; PROTEIN SERINE THREONINE KINASE;

AMINO ACID ANALYSIS; ARTICLE; AUTOPHOSPHORYLATION; CONTROLLED STUDY; DISEASE RESISTANCE; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME LOCALIZATION; ENZYME PHOSPHORYLATION; ESCHERICHIA COLI; PRIORITY JOURNAL; PROTEIN EXPRESSION; SIGNAL TRANSDUCTION; SITE DIRECTED MUTAGENESIS; TOMATO;

AMINO ACID SEQUENCE; BINDING SITES; ESCHERICHIA COLI; LYCOPERSICON ESCULENTUM; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDE MAPPING; PHOSPHOPEPTIDES; PHOSPHORYLATION; PLANT PROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; THREONINE; TRYPSIN; TWO-HYBRID SYSTEM TECHNIQUES;

EID: 0033962918     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.00979.x     Document Type: Article

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