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Plant Physiol, November 1999, Vol. 121, pp. 813-820
Sucrose and Cytokinin Modulation of WPK4, a Gene
Encoding a SNF1-Related Protein Kinase from Wheat1
Yoshihisa
Ikeda,
Nozomu
Koizumi,
Tomonobu
Kusano, and
Hiroshi
Sano*
Laboratory of Plant Molecular Breeding, Research and Education
Center for Genetic Information, Nara Institute of Science and
Technology, Ikoma, Nara 630-0101, Japan
WPK4, a gene encoding
a putative protein kinase, was initially identified in wheat
(Triticum aestivum) and shown to be up-regulated by
light, nutrient deprivation, and cytokinins. To confirm that WPK4 has
protein kinase activity, the protein was produced in Escherichia
coli as a fusion protein with glutathione
S-transferase. The purified protein exhibited
autophosphorylation activity and phosphorylated both myelin basic
protein and a peptide fragment of rice
3-hydroxy-3-methylglutaryl-coenzyme A reductase. Levels of
WPK4 transcripts in wheat seedlings were increased and
decreased by the removal and addition of sucrose (Suc), respectively,
to the culture medium. The introduction of the N-terminal kinase region
of WPK4 into the yeast snf1 mutant cells, which cannot utilize Suc as a carbon source, rescued growth in Suc-containing medium. Cytokinins up-regulated the accumulation of WPK4
transcripts, but their effects were cancelled by the addition of Suc.
Our results suggest that Suc negatively regulates the signaling pathway
in which transcriptional activation of WPK4 is mediated
by cytokinins.
1
This work was supported by a Grant-in-Aid
(no. 09274102) from the Ministry of Education, Science, Sports
and Culture of Japan.
*
Corresponding author; e-mail sano{at}bs.aist-nara.ac.jp; fax
81-743-72-5659.
© 1999 American Society of Plant Physiologists
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