A plant receptor-like gene, the S-locus receptor kinase of Brassica oleracea L., encodes a functional serine/threonine kinase

To investigate the catalytic properties of the Brassica oleracea S-locus receptor kinase (SRK), we have expressed the domain that is homologous to protein kinases as a fusion protein in Escherichia coli. Following in vivo labeling of cultures with 32P-labeled inorganic phosphate, we observed phospho...

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Bibliographic Details
Published in:Plant physiology (Bethesda) 1993-03, Vol.101 (3), p.1103-1106
Main Authors: Stein, J.C, Nasrallah, J.B
Format: Article
Language:English
Subjects:
550200 - Biochemistry
550400 - Genetics
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
Amino Acid Sequence
AMINO ACIDS
ARGININE
Autoradiography
Base Sequence
BASIC BIOLOGICAL SCIENCES
Binding Sites
Biological and medical sciences
BIOLOGICAL EFFECTS
BRASSICA
Brassica - enzymology
Brassica - genetics
BRASSICA OLERACEA
CARBOXYLIC ACIDS
CATABOLISM
CHEMICAL REACTIONS
CHIMIORECEPTEUR
Codons
CONTROL
DNA
ENZYMES
ESCHERICHIA
Escherichia coli
FOOD
FOSFORILACION
Fundamental and applied biological sciences. Psychology
GENE
Gene expression
GENES
Genes, Plant
GENETIC CONTROL
Genetic mutation
HYDROXY ACIDS
IN VIVO
LYSINE
MAGNOLIOPHYTA
MAGNOLIOPSIDA
METABOLISM
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
ORGANIC ACIDS
ORGANIC COMPOUNDS
PEST CONTROL
Phosphoamino acids
PHOSPHORUS-GROUP TRANSFERASES
PHOSPHORYLATION
PHOSPHOTRANSFERASES
Plant Proteins
PLANTS
Plasmids
Polymerase chain reaction
Protein Kinases - genetics
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
PROTEINA QUINASA
PROTEINE KINASE
PROTEINS
QUIMIORECEPTORS
Rapid Communications
Receptors
SERINA
SERINE
THREONINE
TRANSFERASES
TRANSFERENCIA DE GENES
TRANSFERT DE GENE
TRANSFORMACION GENETICA
TRANSFORMATION GENETIQUE
TREONINA
TYROSINE
VEGETABLES
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Summary:To investigate the catalytic properties of the Brassica oleracea S-locus receptor kinase (SRK), we have expressed the domain that is homologous to protein kinases as a fusion protein in Escherichia coli. Following in vivo labeling of cultures with 32P-labeled inorganic phosphate, we observed phosphorylation of the fusion protein on serine and threonine, but not on tyrosine. In contrast, labeling was not observed when lysine-524, a residue conserved among all protein kinases, was mutated to arginine, thus confirming that SRK phosphorylation was the result of intrinsic serine/threonine kinase activity
ISSN:0032-0889
1532-2548
DOI:10.1104/pp.101.3.1103