Light activates a 46-kDa MAP kinase-like protein kinase in soybean cell culture.
Light induced rapid and transient activation of a 46-kDa protein kinase in soybean photomixotrophic cell culture. This kinase was designated as LAP kinase (light signal-activated protein kinase). Activation of LAP kinase in response to light was associated with tyrosine phosphorylation of the kinase, and treatment of the kinase with protein tyrosine phosphatase abolished its activity. The LAP kinase efficiently phosphorylated myelin basic protein and histone, but did not phosphorylate casein. Phospho-amino acid analysis indicated that the LAP kinase was a serine/threonine protein kinase. These results indicated that the LAP kinase is related to the MAP kinase family of protein kinases.
Yamagata
H
H
Laboratory of Biochemistry, Faculty of Agriculture, Kobe University, Rokkodai-cho 1, Nada-ku, 657-8501, Kobe, Japan. yamagata@kobe-u.ac.jp
Saka
K
K
Tanaka
T
T
Aizono
Y
Y
D002478:Cells, Cultured; D004789:Enzyme Activation; D008027:Light; D020928:Mitogen-Activated Protein Kinases / Q000378:metabolism*; D004676:Myelin Basic Protein / Q000378:metabolism; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D013025:Glycine max / Q000201:enzymology*; D014443:Tyrosine / Q000378:metabolism
D004676:Myelin Basic Protein; D014443:Tyrosine; D017346:Protein Serine-Threonine Kinases; D020928:Mitogen-Activated Protein Kinases